Journal articles: 'FTSJ1'

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Sun, Yangqing, Qingqing Liu, Shangwei Zhong, Rui Wei, and Jun-Li Luo. "Triple-Negative Breast Cancer Intrinsic FTSJ1 Favors Tumor Progression and Attenuates CD8+ T Cell Infiltration." Cancers 16, no. 3 (January 31, 2024): 597. http://dx.doi.org/10.3390/cancers16030597.

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FtsJ RNA 2′-O-methyltransferase 1 (FTSJ1) is a member of the methyltransferase superfamily and is involved in the processing and modification of ribosomal RNA. We herein demonstrate that FTSJ1 favors TNBC progression. The knockdown of FTSJ1 inhibits TNBC cell proliferation and development, induces apoptosis of cancer cells, and increases the sensitivity of TNBC cells to T-cell-mediated cytotoxicity. Furthermore, the high expression of FTSJ1 in TNBC attenuates CD8+T cell infiltration in the tumor microenvironment (TME) correlated with poorer prognosis for clinical TNBC patients. In this study, we establish that FTSJ1 acts as a tumor promotor, is involved in cancer immune evasion, and may serve as a potential immunotherapy target in TNBC.

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Brazane, Mira, Dilyana G. Dimitrova, Julien Pigeon, Chiara Paolantoni, Tao Ye, Virginie Marchand, Bruno Da Silva, et al. "The ribose methylation enzyme FTSJ1 has a conserved role in neuron morphology and learning performance." Life Science Alliance 6, no. 4 (January 31, 2023): e202201877. http://dx.doi.org/10.26508/lsa.202201877.

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FTSJ1 is a conserved human 2′-O-methyltransferase (Nm-MTase) that modifies several tRNAs at position 32 and the wobble position 34 in the anticodon loop. Its loss of function has been linked to X-linked intellectual disability (XLID), and more recently to cancers. However, the molecular mechanisms underlying these pathologies are currently unclear. Here, we report a novelFTSJ1pathogenic variant from an X-linked intellectual disability patient. Using blood cells derived from this patient and other affected individuals carryingFTSJ1mutations, we performed an unbiased and comprehensive RiboMethSeq analysis to map the ribose methylation on all human tRNAs and identify novel targets. In addition, we performed a transcriptome analysis in these cells and found that several genes previously associated with intellectual disability and cancers were deregulated. We also found changes in the miRNA population that suggest potential cross-regulation of some miRNAs with these key mRNA targets. Finally, we show that differentiation of FTSJ1-depleted human neural progenitor cells into neurons displays long and thin spine neurites compared with control cells. These defects are also observed inDrosophilaand are associated with long-term memory deficits. Altogether, our study adds insight into FTSJ1 pathologies in humans and flies by the identification of novel FTSJ1 targets and the defect in neuron morphology.

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von Bohlen und Halbach, Viola, Simone Venz, Simon Nwakor, Christian Hentschker, Elke Hammer, Heike Junker, Andreas Walter Kuss, Oliver von Bohlen und Halbach, and Lars Riff Jensen. "Deficiency in FTSJ1 Affects Neuronal Plasticity in the Hippocampal Formation of Mice." Biology 11, no. 7 (July 5, 2022): 1011. http://dx.doi.org/10.3390/biology11071011.

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The role of the tRNA methyltransferase FTSJ1 in the brain is largely unknown. We analyzed whether FTSJ1-deficient mice (KO) displayed altered neuronal plasticity. We explored open field behavior (10 KO mice (aged 22–25 weeks)) and 11 age-matched control littermates (WT) and examined mean layer thickness (7 KO; 6 WT) and dendritic spines (5 KO; 5 WT) in the hippocampal area CA1 and the dentate gyrus. Furthermore, long-term potentiation (LTP) within area CA1 was investigated (5 KO; 5 WT), and mass spectrometry (MS) using CA1 tissue (2 each) was performed. Compared to controls, KO mice showed a significant reduction in the mean thickness of apical CA1 layers. Dendritic spine densities were also altered in KO mice. Stable LTP could be induced in the CA1 area of KO mice and remained stable at for at least 1 h, although at a lower level as compared to WTs, while MS data indicated differential abundance of several proteins, which play a role in neuronal plasticity. FTSJ1 has an impact on neuronal plasticity in the murine hippocampal area CA1 at the morphological and physiological levels, which, in conjunction with comparable changes in other cortical areas, might accumulate in disturbed learning and memory functions.

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Carollo, Pietro Salvatore, Marco Tutone, Giulia Culletta, Ignazio Fiduccia, Federica Corrao, Ivana Pibiri, Aldo Di Leonardo, et al. "Investigating the Inhibition of FTSJ1, a Tryptophan tRNA-Specific 2′-O-Methyltransferase by NV TRIDs, as a Mechanism of Readthrough in Nonsense Mutated CFTR." International Journal of Molecular Sciences 24, no. 11 (June 1, 2023): 9609. http://dx.doi.org/10.3390/ijms24119609.

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Cystic Fibrosis (CF) is an autosomal recessive genetic disease caused by mutations in the CFTR gene, coding for the CFTR chloride channel. About 10% of the CFTR gene mutations are “stop” mutations that generate a premature termination codon (PTC), thus synthesizing a truncated CFTR protein. A way to bypass PTC relies on ribosome readthrough, which is the ribosome’s capacity to skip a PTC, thus generating a full-length protein. “TRIDs” are molecules exerting ribosome readthrough; for some, the mechanism of action is still under debate. We investigate a possible mechanism of action (MOA) by which our recently synthesized TRIDs, namely NV848, NV914, and NV930, could exert their readthrough activity by in silico analysis and in vitro studies. Our results suggest a likely inhibition of FTSJ1, a tryptophan tRNA-specific 2′-O-methyltransferase.

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Angelova, Margarita T., Dilyana G. Dimitrova, Bruno Da Silva, Virginie Marchand, Caroline Jacquier, Cyrinne Achour, Mira Brazane, et al. "tRNA 2′-O-methylation by a duo of TRM7/FTSJ1 proteins modulates small RNA silencing in Drosophila." Nucleic Acids Research 48, no. 4 (January 16, 2020): 2050–72. http://dx.doi.org/10.1093/nar/gkaa002.

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Abstract 2′-O-Methylation (Nm) represents one of the most common RNA modifications. Nm affects RNA structure and function with crucial roles in various RNA-mediated processes ranging from RNA silencing, translation, self versus non-self recognition to viral defense mechanisms. Here, we identify two Nm methyltransferases (Nm-MTases) in Drosophila melanogaster (CG7009 and CG5220) as functional orthologs of yeast TRM7 and human FTSJ1. Genetic knockout studies together with MALDI-TOF mass spectrometry and RiboMethSeq mapping revealed that CG7009 is responsible for methylating the wobble position in tRNAPhe, tRNATrp and tRNALeu, while CG5220 methylates position C32 in the same tRNAs and also targets additional tRNAs. CG7009 or CG5220 mutant animals were viable and fertile but exhibited various phenotypes such as lifespan reduction, small RNA pathways dysfunction and increased sensitivity to RNA virus infections. Our results provide the first detailed characterization of two TRM7 family members in Drosophila and uncover a molecular link between enzymes catalyzing Nm at specific tRNAs and small RNA-induced gene silencing pathways.

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Dai, Ling, Lianxi Xing, Pingyuan Gong, Kejin Zhang, Xiaocai Gao, Zijian Zheng, Jianping Zhou, Yale Guo, Shaoping Guo, and Fuchang Zhang. "Positive association of the FTSJ1 gene polymorphisms with nonsyndromic X-linked mental retardation in young Chinese male subjects." Journal of Human Genetics 53, no. 7 (April 10, 2008): 592–97. http://dx.doi.org/10.1007/s10038-008-0287-x.

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Jensen, Lars R., Lillian Garrett, Sabine M. Hölter, Birgit Rathkolb, Ildikó Rácz, Thure Adler, Cornelia Prehn, et al. "A mouse model for intellectual disability caused by mutations in the X-linked 2′‑O‑methyltransferase Ftsj1 gene." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1865, no. 9 (September 2019): 2083–93. http://dx.doi.org/10.1016/j.bbadis.2018.12.011.

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Freude, Kristine, Kirsten Hoffmann, Lars-Riff Jensen, Martin B. Delatycki, Vincent des Portes, Bettina Moser, Ben Hamel, et al. "Mutations in the FTSJ1 Gene Coding for a Novel S-Adenosylmethionine–Binding Protein Cause Nonsyndromic X-Linked Mental Retardation." American Journal of Human Genetics 75, no. 2 (August 2004): 305–9. http://dx.doi.org/10.1086/422507.

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Fradejas-Villar, Noelia, Simon Bohleber, Wenchao Zhao, Uschi Reuter, Annika Kotter, Mark Helm, Rainer Knoll, et al. "The Effect of tRNA[Ser]Sec Isopentenylation on Selenoprotein Expression." International Journal of Molecular Sciences 22, no. 21 (October 23, 2021): 11454. http://dx.doi.org/10.3390/ijms222111454.

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Transfer RNA[Ser]Sec carries multiple post-transcriptional modifications. The A37G mutation in tRNA[Ser]Sec abrogates isopentenylation of base 37 and has a profound effect on selenoprotein expression in mice. Patients with a homozygous pathogenic p.R323Q variant in tRNA-isopentenyl-transferase (TRIT1) show a severe neurological disorder, and hence we wondered whether selenoprotein expression was impaired. Patient fibroblasts with the homozygous p.R323Q variant did not show a general decrease in selenoprotein expression. However, recombinant human TRIT1R323Q had significantly diminished activities towards several tRNA substrates in vitro. We thus engineered mice conditionally deficient in Trit1 in hepatocytes and neurons. Mass-spectrometry revealed that hypermodification of U34 to mcm5Um occurs independently of isopentenylation of A37 in tRNA[Ser]Sec. Western blotting and 75Se metabolic labeling showed only moderate effects on selenoprotein levels and 75Se incorporation. A detailed analysis of Trit1-deficient liver using ribosomal profiling demonstrated that UGA/Sec re-coding was moderately affected in Selenop, Txnrd1, and Sephs2, but not in Gpx1. 2′O-methylation of U34 in tRNA[Ser]Sec depends on FTSJ1, but does not affect UGA/Sec re-coding in selenoprotein translation. Taken together, our results show that a lack of isopentenylation of tRNA[Ser]Sec affects UGA/Sec read-through but differs from a A37G mutation.

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Hirata, Akira, Keisuke Okada, Kazuaki Yoshii, Hiroyuki Shiraishi, Shinya Saijo, Kento Yonezawa, Nobutaka Shimizu, and Hiroyuki Hori. "Structure of tRNA methyltransferase complex of Trm7 and Trm734 reveals a novel binding interface for tRNA recognition." Nucleic Acids Research 47, no. 20 (October 5, 2019): 10942–55. http://dx.doi.org/10.1093/nar/gkz856.

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Abstract The complex between Trm7 and Trm734 (Trm7–Trm734) from Saccharomyces cerevisiae catalyzes 2′-O-methylation at position 34 in tRNA. We report biochemical and structural studies of the Trm7–Trm734 complex. Purified recombinant Trm7–Trm734 preferentially methylates tRNAPhe transcript variants possessing two of three factors (Cm32, m1G37 and pyrimidine34). Therefore, tRNAPhe, tRNATrp and tRNALeu are specifically methylated by Trm7–Trm734. We have solved the crystal structures of the apo and S-adenosyl-L-methionine bound forms of Trm7–Trm734. Small angle X-ray scattering reveals that Trm7–Trm734 exists as a hetero-dimer in solution. Trm7 possesses a Rossmann-fold catalytic domain, while Trm734 consists of three WD40 β-propeller domains (termed BPA, BPB and BPC). BPA and BPC form a unique V-shaped cleft, which docks to Trm7. The C-terminal region of Trm7 is required for binding to Trm734. The D-arm of substrate tRNA is required for methylation by Trm7–Trm734. If the D-arm in tRNAPhe is docked onto the positively charged area of BPB in Trm734, the anticodon-loop is located near the catalytic pocket of Trm7. This model suggests that Trm734 is required for correct positioning of tRNA for methylation. Additionally, a point-mutation in Trm7, which is observed in FTSJ1 (human Trm7 ortholog) of nosyndromic X-linked intellectual disability patients, decreases the methylation activity.

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Ramser, J. "A splice site mutation in the methyltransferase gene FTSJ1 in Xp11.23 is associated with non-syndromic mental retardation in a large Belgian family (MRX9)." Journal of Medical Genetics 41, no. 9 (September 1, 2004): 679–83. http://dx.doi.org/10.1136/jmg.2004.019000.

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Froyen, Guy, Marijke Bauters, Jackie Boyle, Hilde Van Esch, Karen Govaerts, Hans van Bokhoven, Hans-Hilger Ropers, et al. "Loss of SLC38A5 and FTSJ1 at Xp11.23 in three brothers with non-syndromic mental retardation due to a microdeletion in an unstable genomic region." Human Genetics 121, no. 5 (February 28, 2007): 539–47. http://dx.doi.org/10.1007/s00439-007-0343-1.

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El-Kafafi, El-Sayed, Mohamed Karamoko, Isabelle Pignot-Paintrand, Didier Grunwald, Paul Mandaron, Silva Lerbs-Mache, and Denis Falconet. "Developmentally regulated association of plastid division protein FtsZ1 with thylakoid membranes in Arabidopsis thaliana." Biochemical Journal 409, no. 1 (December 11, 2007): 87–94. http://dx.doi.org/10.1042/bj20070543.

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FtsZ is a key protein involved in bacterial and organellar division. Bacteria have only one ftsZ gene, while chlorophytes (higher plants and green alga) have two distinct FtsZ gene families, named FtsZ1 and FtsZ2. This raises the question of why chloroplasts in these organisms need distinct FtsZ proteins to divide. In order to unravel new functions associated with FtsZ proteins, we have identified and characterized an Arabidopsis thaliana FtsZ1 loss-of-function mutant. ftsZ1-knockout mutants are impeded in chloroplast division, and division is restored when FtsZ1 is expressed at a low level. FtsZ1-overexpressing plants show a drastic inhibition of chloroplast division. Chloroplast morphology is altered in ftsZ1, with chloroplasts having abnormalities in the thylakoid membrane network. Overexpression of FtsZ1 also induced defects in thylakoid organization with an increased network of twisting thylakoids and larger grana. We show that FtsZ1, in addition to being present in the stroma, is tightly associated with the thylakoid fraction. This association is developmentally regulated since FtsZ1 is found in the thylakoid fraction of young developing plant leaves but not in mature and old plant leaves. Our results suggest that plastid division protein FtsZ1 may have a function during leaf development in thylakoid organization, thus highlighting new functions for green plastid FtsZ.

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TerBush, Allan D., and Katherine W. Osteryoung. "Distinct functions of chloroplast FtsZ1 and FtsZ2 in Z-ring structure and remodeling." Journal of Cell Biology 199, no. 4 (November 5, 2012): 623–37. http://dx.doi.org/10.1083/jcb.201205114.

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FtsZ, a cytoskeletal GTPase, forms a contractile ring for cell division in bacteria and chloroplast division in plants. Whereas bacterial Z rings are composed of a single FtsZ, those in chloroplasts contain two distinct FtsZ proteins, FtsZ1 and FtsZ2, whose functional relationship is poorly understood. We expressed fluorescently tagged FtsZ1 and FtsZ2 in fission yeast to investigate their intrinsic assembly and dynamic properties. FtsZ1 and FtsZ2 formed filaments with differing morphologies when expressed separately. FRAP showed that FtsZ2 filaments were less dynamic than FtsZ1 filaments and that GTPase activity was essential for FtsZ2 filament turnover but may not be solely responsible for FtsZ1 turnover. When coexpressed, the proteins colocalized, consistent with coassembly, but exhibited an FtsZ2-like morphology. However, FtsZ1 increased FtsZ2 exchange into coassembled filaments. Our findings suggest that FtsZ2 is the primary determinant of chloroplast Z-ring structure, whereas FtsZ1 facilitates Z-ring remodeling. We also demonstrate that ARC3, a regulator of chloroplast Z-ring positioning, functions as an FtsZ1 assembly inhibitor.

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EL-KAFAFI, El-Sayed, Sunil MUKHERJEE, Mahmoud EL-SHAMI, Jean-Luc PUTAUX, Maryse A. BLOCK, Isabelle PIGNOT-PAINTRAND, Silva LERBS-MACHE, and Denis FALCONET. "The plastid division proteins, FtsZ1 and FtsZ2, differ in their biochemical properties and sub-plastidial localization." Biochemical Journal 387, no. 3 (April 26, 2005): 669–76. http://dx.doi.org/10.1042/bj20041281.

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Plastid division in higher plants is morphologically similar to bacterial cell division, with a process termed binary fission involving constriction of the envelope membranes. FtsZ proteins involved in bacterial division are also present in higher plants, in which the ftsZ genes belong to two distinct families: ftsZ1 and ftsZ2. However, the roles of the corresponding proteins FtsZ1 and FtsZ2 in plastid division have not been determined. Here we show that the expression of plant FtsZ1 and FtsZ2 in bacteria has different effects on cell division, and that distinct protein domains are involved in the process. We have studied the assembly of purified FtsZ1 and FtsZ2 using a chemical cross-linking approach followed by PAGE and electron microscopy analyses of the resulting polymers. This has revealed that FtsZ1 is capable of forming long rod-shaped polymers and rings similar to the bacterial FtsZ structures, whereas FtsZ2 does not form any organized polymer. Moreover, using purified sub-plastidial fractions, we show that both proteins are present in the stroma, and that a subset of FtsZ2 is tightly bound to the purified envelope membranes. These results indicate that FtsZ2 has a localization pattern distinct from that of FtsZ1, which can be related to distinct properties of the proteins. From the results presented here, we propose a model for the sequential topological localization and functions of green plant FtsZ1 and FtsZ2 in chloroplast division.

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Mcandrew, Rosemary S., Bradley J. S. C. Olson, Deena K. Kadirjan-Kalbach, Cecilia L. Chi-Ham, Stanislav Vitha, John E. Froehlich, and Katherine W. Osteryoung. "In vivo quantitative relationship between plastid division proteins FtsZ1 and FtsZ2 and identification of ARC6 and ARC3 in a native FtsZ complex." Biochemical Journal 412, no. 2 (May 14, 2008): 367–78. http://dx.doi.org/10.1042/bj20071354.

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FtsZ1 and FtsZ2 are phylogenetically distinct homologues of the tubulin-like bacterial cell division protein FtsZ that play major roles in the initiation and progression of plastid division in plant cells. Both proteins are components of a mid-plastid ring, the Z-ring, which functions as a contractile ring on the stromal surface of the chloroplast IEM (inner envelope membrane). FtsZ1 and FtsZ2 have been shown to interact, but their in vivo biochemical properties are largely unknown. To gain insight into the in vivo biochemical relationship between FtsZ1 and FtsZ2, in the present study we investigated their molecular levels in wild-type Arabidopsis thaliana plants and endogenous interactions in Arabidopsis and pea. Quantitative immunoblotting and morphometric analysis showed that the average total FtsZ concentration in chloroplasts of 3-week-old Arabidopsis plants is comparable with that in Escherichia coli. FtsZ levels declined as plants matured, but the molar ratio between FtsZ1 and FtsZ2 remained constant at approx. 1:2, suggesting that this stoichiometry is regulated and functionally important. Density-gradient centrifugation, native gel electrophoresis, gel filtration and co-immunoprecipitation experiments showed that a portion of the FtsZ1 and FtsZ2 in Arabidopsis and pea chloroplasts is stably associated in a complex of ∼200–245 kDa. This complex also contains the FtsZ2-interacting protein ARC6 (accumulation and replicatioin of chloroplasts 6), an IEM protein, and analysis of density-gradient fractions suggests the presence of the FtsZ1-interacting protein ARC3. Based on the mid-plastid localization of ARC6 and ARC3 and their postulated roles in promoting and inhibiting chloroplast FtsZ polymer formation respectively, we hypothesize that the FtsZ1–FtsZ2–ARC3–ARC6 complex represents an unpolymerized IEM-associated pool of FtsZ that contributes to the dynamic regulation of Z-ring assembly and remodelling at the plastid division site in vivo.

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Xu, Kai, Yujin Wu, Jurong Song, Kaining Hu, Zengxiang Wu, Jing Wen, Bin Yi, et al. "Fine Mapping and Identification of BnaC06.FtsH1, a Lethal Gene That Regulates the PSII Repair Cycle in Brassica napus." International Journal of Molecular Sciences 22, no. 4 (February 19, 2021): 2087. http://dx.doi.org/10.3390/ijms22042087.

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Photosystem II (PSII) is an important component of the chloroplast. The PSII repair cycle is crucial for the relief of photoinhibition and may be advantageous when improving stress resistance and photosynthetic efficiency. Lethal genes are widely used in the efficiency detection and method improvement of gene editing. In the present study, we identified the naturally occurring lethal mutant 7-521Y with etiolated cotyledons in Brassica napus, controlled by double-recessive genes (named cyd1 and cyd2). By combining whole-genome resequencing and map-based cloning, CYD1 was fine-mapped to a 29 kb genomic region using 15,167 etiolated individuals. Through cosegregation analysis and functional verification of the transgene, BnaC06.FtsH1 was determined to be the target gene; it encodes an filamentation temperature sensitive protein H 1 (FtsH1) hydrolase that degrades damaged PSII D1 in Arabidopsis thaliana. The expression of BnaC06.FtsH1 was high in the cotyledons, leaves, and flowers of B. napus, and localized in the chloroplasts. In addition, the expression of EngA (upstream regulation gene of FtsH) increased and D1 decreased in 7-521Y. Double mutants of FtsH1 and FtsH5 were lethal in A. thaliana. Through phylogenetic analysis, the loss of FtsH5 was identified in Brassica, and the remaining FtsH1 was required for PSII repair cycle. CYD2 may be a homologous gene of FtsH1 on chromosome A07 of B. napus. Our study provides new insights into lethal mutants, the findings may help improve the efficiency of the PSII repair cycle and biomass accumulation in oilseed rape.

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TerBush, Allan D., Chris A. Porzondek, and Katherine W. Osteryoung. "Functional Analysis of the Chloroplast Division Complex UsingSchizosaccharomyces pombeas a Heterologous Expression System." Microscopy and Microanalysis 22, no. 2 (February 26, 2016): 275–89. http://dx.doi.org/10.1017/s1431927616000143.

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AbstractChloroplast division is driven by a macromolecular complex that assembles at the midplastid. The FtsZ ring (Z ring) is the central structure in this complex, and is composed of the functionally distinct cytoskeletal proteins FtsZ1 and FtsZ2. Recent studies in the heterologousSchizosaccharomyces pombesystem showed that Arabidopsis FtsZ1 and FtsZ2 filaments have distinct assembly and turnover characteristics. To further analyze these FtsZs, we employed this system to compare the assembly and dynamic properties of FtsZ1 and FtsZ2 lacking their N- and/or C-termini with those of their full-length counterparts. Our data provide evidence that the N-terminus of FtsZ2 is critical for its structural dominance over FtsZ1, and that the N- and C-termini promote polymer bundling and turnover of both FtsZs and contribute to their distinct behaviors. We also assessed how ARC6 affects FtsZ2 filament dynamics, and found that it interacts with and stabilizes FtsZ2 filaments inS. pombeindependent of its presumed Z-ring tethering functionin planta. Finally, we generated FtsZ1-FtsZ2 coexpression constructs to facilitate reconstitution of more complex interaction networks. Our experiments yield new insight into factors influencing FtsZ behavior and highlight the utility ofS. pombefor analyzing chloroplast FtsZs and their assembly regulators.

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Vitha, Stanislav, Rosemary S. McAndrew, and Katherine W. Osteryoung. "Ftsz Ring Formation at the Chloroplast Division Site in Plants." Journal of Cell Biology 153, no. 1 (April 2, 2001): 111–20. http://dx.doi.org/10.1083/jcb.153.1.111.

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Among the events that accompanied the evolution of chloroplasts from their endosymbiotic ancestors was the host cell recruitment of the prokaryotic cell division protein FtsZ to function in chloroplast division. FtsZ, a structural homologue of tubulin, mediates cell division in bacteria by assembling into a ring at the midcell division site. In higher plants, two nuclear-encoded forms of FtsZ, FtsZ1 and FtsZ2, play essential and functionally distinct roles in chloroplast division, but whether this involves ring formation at the division site has not been determined previously. Using immunofluorescence microscopy and expression of green fluorescent protein fusion proteins in Arabidopsis thaliana, we demonstrate here that FtsZ1 and FtsZ2 localize to coaligned rings at the chloroplast midpoint. Antibodies specific for recognition of FtsZ1 or FtsZ2 proteins in Arabidopsis also recognize related polypeptides and detect midplastid rings in pea and tobacco, suggesting that midplastid ring formation by FtsZ1 and FtsZ2 is universal among flowering plants. Perturbation in the level of either protein in transgenic plants is accompanied by plastid division defects and assembly of FtsZ1 and FtsZ2 into filaments and filament networks not observed in wild-type, suggesting that previously described FtsZ-containing cytoskeletal-like networks in chloroplasts may be artifacts of FtsZ overexpression.

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Liu, Xiaomin, Jinjie An, Lulu Wang, Qingqing Sun, Chuanjing An, Bibo Wu, Conghao Hong, et al. "A novel amphiphilic motif at the C-terminus of FtsZ1 facilitates chloroplast division." Plant Cell 34, no. 1 (November 10, 2021): 419–32. http://dx.doi.org/10.1093/plcell/koab272.

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Abstract In bacteria and chloroplasts, the GTPase filamentous temperature-sensitive Z (FtsZ) is essential for division and polymerizes to form rings that mark the division site. Plants contain two FtsZ subfamilies (FtsZ1 and FtsZ2) with different assembly dynamics. FtsZ1 lacks the C-terminal domain of a typical FtsZ protein. Here, we show that the conserved short motif FtsZ1 Carboxyl-terminus (Z1C) (consisting of the amino acids RRLFF) with weak membrane-binding activity is present at the C-terminus of FtsZ1 in angiosperms. For a polymer-forming protein such as FtsZ, this activity is strong enough for membrane tethering. Arabidopsis thaliana plants with mutated Z1C motifs contained heterogeneously sized chloroplasts and parallel FtsZ rings or long FtsZ filaments, suggesting that the Z1C motif plays an important role in regulating FtsZ ring dynamics. Our findings uncover a type of amphiphilic beta-strand motif with weak membrane-binding activity and point to the importance of this motif for the dynamic regulation of protein complex formation.

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Abrams, Sydney R., Alexandra L. Hawks, Jacquelyn M. Evans, Thomas R. Famula, Mary Mahaffey, Gary S. Johnson, Jennifer M. Mason, and Leigh Anne Clark. "Variants in FtsJ RNA 2′-O-Methyltransferase 3 and Growth Hormone 1 are associated with small body size and a dental anomaly in dogs." Proceedings of the National Academy of Sciences 117, no. 40 (September 21, 2020): 24929–35. http://dx.doi.org/10.1073/pnas.2009500117.

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Domesticated dogs show unparalleled diversity in body size across breeds, but within breeds variation is limited by selective breeding. Many heritable diseases of dogs are found among breeds of similar sizes, suggesting that as in humans, alleles governing growth have pleiotropic effects. Here, we conducted independent genome-wide association studies in the small Shetland Sheepdog breed and discovered a locus on chromosome 9 that is associated with a dental abnormality called maxillary canine-tooth mesioversion (MCM) (P = 1.53 × 10−7) as well as two body size traits: height (P = 1.67 × 10−5) and weight (P = 1.16 × 10−7). Using whole-genome resequencing data, we identified variants in two proximal genes: FTSJ3, encoding an RNA methyltransferase, and GH1, encoding growth hormone. A substitution in FTSJ3 and a splice donor insertion in GH1 are strongly associated with MCM and reduced body size in Shetland Sheepdogs. We demonstrated in vitro that the GH1 variant leads to exon 3 skipping, predicting a mutant protein known to cause human pituitary dwarfism. Statistical modeling, however, indicates that the FTSJ3 variant is the stronger predictor of MCM and that each derived allele reduces body size by about 1 inch and 5 pounds. In a survey of 224 breeds, both FTSJ3 and GH1 variants are frequent among very small “toy” breeds and absent from larger breeds. Our findings indicate that a chromosome 9 locus harboring tightly linked variants in FTSJ3 and GH1 reduces growth in the Shetland Sheepdog and toy breed dogs and confers risk for MCM through vertical pleiotropy.

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Pfotenhauer, Alexander C., Alessandro Occhialini, Stacee A. Harbison, Li Li, Agnieszka A. Piatek, Curtis R. Luckett, Yongil Yang, C. Neal Stewart, and Scott C. Lenaghan. "Genome-Editing of FtsZ1 for Alteration of Starch Granule Size in Potato Tubers." Plants 12, no. 9 (May 4, 2023): 1878. http://dx.doi.org/10.3390/plants12091878.

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Genome-editing has enabled rapid improvement for staple food crops, such as potato, a key beneficiary of the technology. In potato, starch contained within tubers represents the primary product for use in food and non-food industries. Starch granules are produced in the plastids of tubers with plastid size correlated with the size of starch grana. The division of plastids is controlled by proteins, including the tubulin-like GTPase FtsZ1. The altered expression of FtsZ1 has been shown to disrupt plastid division, leading to the production of “macro-plastid”-containing plants. These macro-chloroplast plants are characterized by cells containing fewer and enlarged plastids. In this work, we utilize CRISPR/Cas9 to generate FtsZ1 edited potato lines to demonstrate that genome-editing can be used to increase the size of starch granules in tubers. Altered plastid morphology was comparable to the overexpression of FtsZ1 in previous work in potato and other crops. Several lines were generated with up to a 1.98-fold increase in starch granule size that was otherwise phenotypically indistinguishable from wild-type plants. Further, starch paste from one of the most promising lines showed a 2.07-fold increase in final viscosity. The advantages of enlarged starch granules and the potential of CRISPR/Cas9-based technologies for food crop improvement are further discussed.

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Xing, Shenghui, Wenjia Zheng, Fang An, Leqi Huang, Xinwei Yang, Shuang Zeng, Ningning Li, Khadidja Ouenzar, Liangliang Yu, and Li Luo. "Transcription Regulation of Cell Cycle Regulatory Genes Mediated by NtrX to Affect Sinorhizobium meliloti Cell Division." Genes 13, no. 6 (June 15, 2022): 1066. http://dx.doi.org/10.3390/genes13061066.

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The cell division of the alfalfa symbiont, Sinorhizobium meliloti, is dictated by a cell cycle regulatory pathway containing the key transcription factors CtrA, GcrA, and DnaA. In this study, we found that NtrX, one of the regulators of nitrogen metabolism, can directly regulate the expression of ctrA, gcrA, and dnaA from the cell cycle pathway. Three sets of S. meliloti ntrX mutants showed similar cell division defects, such as slow growth, abnormal morphology of some cells, and delayed DNA synthesis. Transcription of ctrA and gcrA was upregulated, whereas the transcription of dnaA and ftsZ1 was downregulated in the insertion mutant and the strain of Sm1021 expressing ntrXD53E. Correspondingly, the inducible transcription of ntrX activates the expression of dnaA and ftsZ1, but represses ctrA and gcrA in the depletion strain. The expression levels of CtrA and GcrA were confirmed by Western blotting. The transcription regulation of these genes requires phosphorylation of the conserved 53rd aspartate in the NtrX protein that binds directly to the promoter regions of ctrA, gcrA, dnaA, and ftsZ1 by recognizing the characteristic sequence CAAN2-5TTG. Our findings suggest that NtrX affects S. meliloti cell division by regulating the transcription of the key cell cycle regulatory genes.

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Johnson, Carol B., Rahamthulla Shaik, Rehab Abdallah, Stanislav Vitha, and Andreas Holzenburg. "FtsZ1/FtsZ2 Turnover in Chloroplasts and the Role of ARC3." Microscopy and Microanalysis 21, no. 2 (March 3, 2015): 313–23. http://dx.doi.org/10.1017/s1431927615000082.

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AbstractChloroplast division requires filamentation temperature-sensitive Z (FtsZ), a tubulin-like GTPase of cyanobacterial endosymbiotic origin. Plants and algae possess two distinct FtsZ protein families, FtsZ1 and FtsZ2 that co-assemble into a ring (Z-ring) at the division site. Z-ring assembly and disassembly and division site positioning is controlled by both positive and negative factors via their specific interactions with FtsZ1 and FtsZ2. Here we present thein plantaanalysis ofArabidopsisFtsZ1 and FtsZ2 turnover in the context of a native chloroplast division machinery. Fluorescence recovery after photobleaching analysis was conducted using fluorescently tagged FtsZ at wild-type (WT)-like levels. Rapid photobleaching, low signal-to-noise ratio, and phototropic movements of chloroplasts were overcome by (i) using progressive intervals in time-lapse imaging, (ii) analyzing epidermal rather than stromal chloroplasts, and (iii) employing image stack alignment during postprocessing. In plants of WT background, fluorescence recovery half-times averaged 117 and 325 s for FtsZ1 and FtsZ2, respectively. In plants lacking ARC3, the key negative regulator of FtsZ assembly, the turnover was threefold slower. The findings are discussed in the context of previous results conducted in a heterologous system.

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Zhao, Wenlong, Huixia Zhu, Feng Wei, Donglai Zhou, Youguo Li, and Xue-Xian Zhang. "Investigating the Involvement of Cytoskeletal Proteins MreB and FtsZ in the Origin of Legume-Rhizobial Symbiosis." Molecular Plant-Microbe Interactions® 34, no. 5 (May 2021): 547–59. http://dx.doi.org/10.1094/mpmi-10-20-0299-fi.

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Rhizobia are rod-shaped bacteria that form nitrogen-fixing root nodules on leguminous plants; however, they don’t carry MreB, a key determinant of rod-like cell shape. Here, we introduced an actin-like mreB homolog from a pseudomonad into Mesorhizobium huakuii 7653R (a microsymbiont of Astragalus sinicus L.) and examined the molecular, cellular, and symbiotic phenotypes of the resultant mutant. Exogenous mreB caused an enlarged cell size and slower growth in laboratory medium. However, the mutant formed small, ineffective nodules on A. sinicus (Nod+ Fix−), and rhizobial cells in the infection zone were unable to differentiate into bacteroids. RNA sequencing analysis also revealed minor effects of mreB on global gene expression in free-living cells but larger effects for cells grown in planta. Differentially expressed nodule-specific genes include cell cycle regulators such as the tubulin-like ftsZ1 and ftsZ2. Unlike the ubiquitous FtsZ1, an FtsZ2 homolog was commonly found in Rhizobium, Sinorhizobium, and Mesorhizobium spp. but not in closely related nonsymbiotic species. Bacterial two-hybrid analysis revealed that MreB interacts with FtsZ1 and FtsZ2, which are targeted by the host-derived nodule-specific cysteine-rich peptides. Significantly, MreB mutation D283A disrupted the protein–protein interactions and restored the aforementioned phenotypic defects caused by MreB in M. huakuii. Together, our data indicate that MreB is detrimental for modern rhizobia and its interaction with FtsZ1 and FtsZ2 causes the symbiotic process to cease at the late stage of bacteroid differentiation. These findings led to a hypothesis that loss of mreB in the common ancestor of members of Rhizobiales and subsequent acquisition of ftsZ2 are critical evolutionary steps leading to legume-rhizobial symbiosis. [Formula: see text] Copyright © 2021 The Author(s). This is an open access article distributed under the CC BY-NC-ND 4.0 International license .

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Liu, Xiaoqiu, Fengying Li, Shu Qiang Sun, Muthusamy Thangavel, Joseph Kaminsky, Louisa Balazs, and Rennolds S. Ostrom. "Fibroblast-specific expression of AC6 enhances β-adrenergic and prostacyclin signaling and blunts bleomycin-induced pulmonary fibrosis." American Journal of Physiology-Lung Cellular and Molecular Physiology 298, no. 6 (June 2010): L819—L829. http://dx.doi.org/10.1152/ajplung.00429.2009.

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Pulmonary fibroblasts regulate extracellular matrix production and degradation and are critical in maintenance of lung structure, function, and repair, but they also play a central role in lung fibrosis. cAMP-elevating agents inhibit cytokine- and growth factor-stimulated myofibroblast differentiation and collagen synthesis in pulmonary fibroblasts. In the present study, we overexpressed adenylyl cyclase 6 (AC6) in pulmonary fibroblasts and measured cAMP production and collagen synthesis. AC6 overexpression enhanced cAMP production and the inhibition of collagen synthesis mediated by isoproterenol and beraprost, but not the responses to butaprost or PGE2. To examine if increased AC6 expression would impact the development of fibrosis in an animal model, we generated transgenic mice that overexpress AC6 under a fibroblast-specific promoter, FTS1. Lung fibrosis was induced in FTS1-AC6+/− mice and littermate controls by intratracheal instillation of saline or bleomycin. Wild-type mice treated with bleomycin showed extensive peribronchial and interstitial fibrosis and collagen deposition. By contrast, FTS1-AC6+/− mice displayed decreased fibrotic development, lymphocyte infiltration (as determined by pathological scoring), and lung collagen content. Thus, AC6 overexpression inhibits fibrogenesis in the lung by reducing pulmonary fibroblast-mediated collagen synthesis and myofibroblast differentiation. Because AC6 overexpression does not lead to enhanced basal or PGE2-stimulated levels of cAMP, we conclude that endogenous catecholamines or prostacyclin is produced during bleomycin-induced lung fibrosis and that these signals have antifibrotic potential.

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Wang, Lulu, Yajuan Chen, Di Niu, Mingdong Tang, Jinjie An, Shanshan Xue, Xiaomin Liu, and Hongbo Gao. "Improvements for Tissue-Chopping-Based Immunofluorescence Staining Method of Chloroplast Proteins." Plants 12, no. 4 (February 13, 2023): 841. http://dx.doi.org/10.3390/plants12040841.

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Immunofluorescence staining is a very common method for the subcellular localization study of proteins. A tissue-chopping-based immunofluorescence staining method for chloroplast proteins overcomes the restriction of plant cell wall, makes the operation simpler, and uses less experimental materials. Here we provide some improvements for this method. We found that the stained tissues can be directly observed with a confocal microscope without tissue lysis. Samples maintained at a low temperature (0–4 °C) throughout the process can reduce the intensity of chlorophyll autofluorescence and the background signal. A low temperature is also good for the storage of the sample. Fluorescence signal of the stained samples can be kept for several weeks if they are stored at −20 °C. FtsZ is an essential component of the chloroplast division apparatus. We demonstrated this method with the immunofluorescence staining of FtsZ1 in wildtype Arabidopsis and some chloroplast division mutants. We also successfully tested this method by the immunofluorescence staining of FtsZ1 in many other plants, including woody plants. With these procedures, the performance of tissue-chopping-based immunofluorescence staining method are further improved.

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Simabuco, Fernando M., Luis G. Morello, Annelize Zambon Barbosa Aragão, Adriana Franco Paes Leme, and Nilson I. T. Zanchin. "Proteomic Characterization of the Human FTSJ3 Preribosomal Complexes." Journal of Proteome Research 11, no. 6 (May 11, 2012): 3112–26. http://dx.doi.org/10.1021/pr201106n.

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Smith, Aaron G., Carol B. Johnson, Stanislav Vitha, and Andreas Holzenburg. "Oligomerization of plant FtsZ1 and FtsZ2 plastid division proteins." Archives of Biochemistry and Biophysics 513, no. 2 (September 2011): 94–101. http://dx.doi.org/10.1016/j.abb.2011.07.001.

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Chen, Joseph C., Michael Minev, and Jon Beckwith. "Analysis of ftsQ Mutant Alleles in Escherichia coli: Complementation, Septal Localization, and Recruitment of Downstream Cell Division Proteins." Journal of Bacteriology 184, no. 3 (February 1, 2002): 695–705. http://dx.doi.org/10.1128/jb.184.3.695-705.2002.

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ABSTRACT FtsQ, a 276-amino-acid, bitopic membrane protein, is one of the nine proteins known to be essential for cell division in gram-negative bacterium Escherichia coli. To define residues in FtsQ critical for function, we performed random mutagenesis on the ftsQ gene and identified four alleles (ftsQ2, ftsQ6, ftsQ15, and ftsQ65) that fail to complement the ftsQ1(Ts) mutation at the restrictive temperature. Two of the mutant proteins, FtsQ6 and FtsQ15, are functional at lower temperatures but are unable to localize to the division site unless wild-type FtsQ is depleted, suggesting that they compete poorly with the wild-type protein for septal targeting. The other two mutants, FtsQ2 and FtsQ65, are nonfunctional at all temperatures tested and have dominant-negative effects when expressed in an ftsQ1(Ts) strain at the permissive temperature. FtsQ2 and FtsQ65 localize to the division site in the presence or absence of endogenous FtsQ, but they cannot recruit downstream cell division proteins, such as FtsL, to the septum. These results suggest that FtsQ2 and FtsQ65 compete efficiently for septal targeting but fail to promote the further assembly of the cell division machinery. Thus, we have separated the localization ability of FtsQ from its other functions, including recruitment of downstream cell division proteins, and are beginning to define regions of the protein responsible for these distinct capabilities.

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Ozawa, Shin-Ichiro, Guoxian Zhang, and Wataru Sakamoto. "Dysfunction of Chloroplast Protease Activity Mitigates pgr5 Phenotype in the Green Algae Chlamydomonas reinhardtii." Plants 13, no. 5 (February 23, 2024): 606. http://dx.doi.org/10.3390/plants13050606.

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Researchers have described protection mechanisms against the photoinhibition of photosystems under strong-light stress. Cyclic Electron Flow (CEF) mitigates electron acceptor-side limitation, and thus contributes to Photosystem I (PSI) protection. Chloroplast protease removes damaged protein to assist with protein turn over, which contributes to the quality control of Photosystem II (PSII). The PGR5 protein is involved in PGR5-dependent CEF. The FTSH protein is a chloroplast protease which effectively degrades the damaged PSII reaction center subunit, D1 protein. To investigate how the PSI photoinhibition phenotype in pgr5 would be affected by adding the ftsh mutation, we generated double-mutant pgr5ftsh via crossing, and its phenotype was characterized in the green algae Chlamydomonas reinhardtii. The cells underwent high-light incubation as well as low-light incubation after high-light incubation. The time course of Fv/Fm values in pgr5ftsh showed the same phenotype with ftsh1-1. The amplitude of light-induced P700 photo-oxidation absorbance change was measured. The amplitude was maintained at a low value in the control and pgr5ftsh during high-light incubation, but was continuously decreased in pgr5. During the low-light incubation after high-light incubation, amplitude was more rapidly recovered in pgr5ftsh than pgr5. We concluded that the PSI photoinhibition by the pgr5 mutation is mitigated by an additional ftsh1-1 mutation, in which plastoquinone pool would be less reduced due to damaged PSII accumulation.

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Leclerc, G., C. Sirard, and G. R. Drapeau. "The Escherichia coli cell division mutation ftsM1 is in serU." Journal of Bacteriology 171, no. 4 (1989): 2090–95. http://dx.doi.org/10.1128/jb.171.4.2090-2095.1989.

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Vitha, S., RS McAndrew, D. Kadirjan-Kalbach, KW Osteryoung, and A. Holzenburg. "Localization and Molecular Stoichiometry of Plastid Division Proteins FtsZ1 and FtsZ2." Microscopy and Microanalysis 12, S02 (July 31, 2006): 456–57. http://dx.doi.org/10.1017/s1431927606063574.

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Ozawa, K., R. Yatsunami, and S. Nakamura. "Gene cloning of ftsZ1 homolog from extremely halophilic archaeon Haloarcula japonica." Nucleic Acids Symposium Series 3, no. 1 (September 1, 2003): 313–14. http://dx.doi.org/10.1093/nass/3.1.313.

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Olson, Bradley J. S. C., Qiang Wang, and Katherine W. Osteryoung. "GTP-dependent Heteropolymer Formation and Bundling of Chloroplast FtsZ1 and FtsZ2." Journal of Biological Chemistry 285, no. 27 (April 26, 2010): 20634–43. http://dx.doi.org/10.1074/jbc.m110.122614.

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Nguyen, Minh Khiem, Tin-Han Shih, Szu-Hsien Lin, Jun-Wei Lin, Hoang Chinh Nguyen, Zhi-Wei Yang, and Chi-Ming Yang. "Transcription Profile Analysis of Chlorophyll Biosynthesis in Leaves of Wild-Type and Chlorophyll b-Deficient Rice (Oryza sativa L.)." Agriculture 11, no. 5 (April 28, 2021): 401. http://dx.doi.org/10.3390/agriculture11050401.

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Photosynthesis is an essential biological process and a key approach for raising crop yield. However, photosynthesis in rice is not fully investigated. This study reported the photosynthetic properties and transcriptomic profiles of chlorophyll (Chl) b-deficient mutant (ch11) and wild-type rice (Oryza sativa L.). Chl b-deficient rice revealed irregular chloroplast development (indistinct membranes, loss of starch granules, thinner grana, and numerous plastoglobuli). Next-generation sequencing approach application revealed that the differential expressed genes were related to photosynthesis machinery, Chl-biosynthesis, and degradation pathway in ch11. Two genes encoding PsbR (PSII core protein), FtsZ1, and PetH genes, were found to be down-regulated. The expression of the FtsZ1 and PetH genes resulted in disrupted chloroplast cell division and electron flow, respectively, consequently reducing Chl accumulation and the photosynthetic capacity of Chl b-deficient rice. Furthermore, this study found the up-regulated expression of the GluRS gene, whereas the POR gene was down-regulated in the Chl biosynthesis and degradation pathways. The results obtained from RT-qPCR analyses were generally consistent with those of transcription analysis, with the exception of the finding that MgCH genes were up-regulated which enhance the important intermediate products in the Mg branch of Chl biosynthesis. These results indicate a reduction in the accumulation of both Chl a and Chl b. This study suggested that a decline in Chl accumulation is caused by irregular chloroplast formation and down-regulation of POR genes; and Chl b might be degraded via the pheophorbide b pathway, which requires further elucidation.

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Lai, Cheng-Wei, Hsiao-Ling Chen, Ken-Yo Lin, Fang-Chueh Liu, Kowit-Yu Chong, Winston T. K. Cheng, and Chuan-Mu Chen. "FTSJ2, a Heat Shock-Inducible Mitochondrial Protein, Suppresses Cell Invasion and Migration." PLoS ONE 9, no. 3 (March 4, 2014): e90818. http://dx.doi.org/10.1371/journal.pone.0090818.

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Tan, Jacqueline, Ursula Jakob, and James C. A. Bardwell. "Overexpression of Two Different GTPases Rescues a Null Mutation in a Heat-Induced rRNA Methyltransferase." Journal of Bacteriology 184, no. 10 (May 15, 2002): 2692–98. http://dx.doi.org/10.1128/jb.184.10.2692-2698.2002.

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ABSTRACT The Escherichia coli RrmJ (FtsJ) heat shock protein functions as an rRNA methyltransferase that modifies position U2552 of 23S rRNA in intact 50S ribosomal subunits. An in-frame deletion of the rrmJ (ftsJ) gene leads to severe growth disadvantages under all temperatures tested and causes significant accumulation of ribosomal subunits at the expense of functional 70S ribosomes. To investigate whether overexpression of other E. coli genes can restore the severe growth defect observed in rrmJ null mutants, we constructed an overexpression library from the rrmJ deletion strain and cloned and identified the E. coli genes that were capable of rescuing the rrmJ mutant phenotype. Our intention was to identify other methylases whose specificities overlapped enough with that of RrmJ to allow complementation when overexpressed. To our great surprise, no methylases were found by this method; rather, two small GTPases, Obg (YhbZ) and EngA, when overexpressed in the rrmJ deletion strains, were found to restore the otherwise severely impaired ribosome assembly process and/or stability of 70S ribosomes. 50S ribosomal subunits prepared from these overexpressing strains were shown to still serve as in vitro substrates for purified RrmJ, indicating that the 23S rRNA likely was still lacking the highly conserved Um2552 modification. The apparent lack of this modification, however, no longer caused ribosome defects or a growth disadvantage. Massive overexpression of another related small GTPase, Era, failed to rescue the growth defects of an rrmJ strain. These findings suggest a hitherto unexpected connection between rRNA methylation and GTPase function, specifically that of the two small GTPases Obg and EngA.

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Porter, Katie J., Lingyan Cao, Yaodong Chen, Allan D. TerBush, Cheng Chen, Harold P. Erickson, and Katherine W. Osteryoung. "The Arabidopsis thaliana chloroplast division protein FtsZ1 counterbalances FtsZ2 filament stability in vitro." Journal of Biological Chemistry 296 (January 2021): 100627. http://dx.doi.org/10.1016/j.jbc.2021.100627.

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Tang, L. Y., N. Nagata, R. Matsushima, Y. Chen, Y. Yoshioka, and W. Sakamoto. "Visualization of Plastids in Pollen Grains: Involvement of FtsZ1 in Pollen Plastid Division." Plant and Cell Physiology 50, no. 4 (March 12, 2009): 904–8. http://dx.doi.org/10.1093/pcp/pcp042.

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Smith, AG, CB Johnson, S. Vitha, and A. Holzenburg. "In Vitro Assembly of the Arabidopsis thaliana Plastid Division Proteins FtsZ1 and FtsZ2." Microscopy and Microanalysis 14, S2 (August 2008): 1496–97. http://dx.doi.org/10.1017/s1431927608082330.

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Johnson, CB, AG Smith, S. Vitha, and A. Holzenburg. "Arabidopsis Plastid Division Proteins FtsZ1 and FtsZ2: Macromolecular Assembly and Subunit Exchange Dynamics." Microscopy and Microanalysis 15, S2 (July 2009): 882–83. http://dx.doi.org/10.1017/s143192760909360x.

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Morello, Luis G., Patricia P. Coltri, Alexandre J. C. Quaresma, Fernando M. Simabuco, Tereza C. L. Silva, Guramrit Singh, Jeffrey A. Nickerson, Carla C. Oliveira, Melissa J. Moore, and Nilson I. T. Zanchin. "The Human Nucleolar Protein FTSJ3 Associates with NIP7 and Functions in Pre-rRNA Processing." PLoS ONE 6, no. 12 (December 16, 2011): e29174. http://dx.doi.org/10.1371/journal.pone.0029174.

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Stokes, Kevin D., and Katherine W. Osteryoung. "Early divergence of the FtsZ1 and FtsZ2 plastid division gene families in photosynthetic eukaryotes." Gene 320 (November 2003): 97–108. http://dx.doi.org/10.1016/s0378-1119(03)00814-x.

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Smith, Aaron G., Carol B. Johnson, Stanislav Vitha, and Andreas Holzenburg. "Plant FtsZ1 and FtsZ2 expressed in a eukaryotic host: GTPase activity and self-assembly." FEBS Letters 584, no. 1 (November 16, 2009): 166–72. http://dx.doi.org/10.1016/j.febslet.2009.11.044.

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Fujiwara, Makoto T., Haruki Hashimoto, Yusuke Kazama, Tomonari Hirano, Yasushi Yoshioka, Seishiro Aoki, Naoki Sato, Ryuuichi D. Itoh, and Tomoko Abe. "Dynamic morphologies of pollen plastids visualised by vegetative-specific FtsZ1–GFP in Arabidopsis thaliana." Protoplasma 242, no. 1-4 (March 1, 2010): 19–33. http://dx.doi.org/10.1007/s00709-010-0119-7.

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Ringeard, Mathieu, Virginie Marchand, Etienne Decroly, Yuri Motorin, and Yamina Bennasser. "FTSJ3 is an RNA 2′-O-methyltransferase recruited by HIV to avoid innate immune sensing." Nature 565, no. 7740 (January 2019): 500–504. http://dx.doi.org/10.1038/s41586-018-0841-4.

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Buddelmeijer, Nienke, Mirjam E. G. Aarsman, Arend H. J. Kolk, Miguel Vicente, and Nanne Nanninga. "Localization of Cell Division Protein FtsQ by Immunofluorescence Microscopy in Dividing and Nondividing Cells ofEscherichia coli." Journal of Bacteriology 180, no. 23 (December 1, 1998): 6107–16. http://dx.doi.org/10.1128/jb.180.23.6107-6116.1998.

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ABSTRACT The localization of cell division protein FtsQ in Escherichia coli wild-type cells was studied by immunofluorescence microscopy with specific monoclonal antibodies. FtsQ could be localized to the division site in constricting cells. FtsQ could also localize to the division site in ftsQ1(Ts) cells grown at the permissive temperature. A hybrid protein in which the cytoplasmic domain and the transmembrane domain were derived from the γ form of penicillin-binding protein 1B and the periplasmic domain was derived from FtsQ was also able to localize to the division site. This result indicates that the periplasmic domain of FtsQ determines the localization of FtsQ, as has also been concluded by others for the periplasmic domain of FtsN. Noncentral FtsQ foci were found in the area of the cell where the nucleoid resides and were therefore assumed to represent sites where the FtsQ protein is synthesized and simultaneously inserted into the cytoplasmic membrane.

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Cooper, Alexei, Andrea M. Makkay, and R. Thane Papke. "Archaeal Tubulin-like Proteins Modify Cell Shape in Haloferax volcanii during Early Biofilm Development." Genes 14, no. 10 (September 25, 2023): 1861. http://dx.doi.org/10.3390/genes14101861.

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Tubulin, an extensively studied self-assembling protein, forms filaments in eukaryotic cells that affect cell shape, among other functions. The model archaeon Haloferax volcanii uses two tubulin-like proteins (FtsZ1/FtsZ2) for cell division, similar to bacteria, but has an additional six related tubulins called CetZ. One of them, CetZ1, was shown to play a role in cell shape. Typically, discoid and rod shapes are observed in planktonic growth, but under biofilm formation conditions (i.e., attached to a substratum), H. volcanii can grow filamentously. Here, we show that the deletion mutants of all eight tubulin-like genes significantly impacted morphology when cells were allowed to form a biofilm. ΔftsZ1, ΔcetZ2, and ΔcetZ4-6 created longer, less round cells than the parental and a higher percentage of filaments. ΔcetZ1 and ΔcetZ3 were significantly rounder than the parental, and ΔftsZ2 generated larger, flat, amorphic cells. The results show all tubulin homologs affect morphology at most timepoints, which therefore suggests these genes indeed have a function.

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Stokes, Kevin D., Rosemary S. McAndrew, Rubi Figueroa, Stanislav Vitha, and Katherine W. Osteryoung. "Chloroplast Division and Morphology Are Differentially Affected by Overexpression of FtsZ1 and FtsZ2 Genes in Arabidopsis." Plant Physiology 124, no. 4 (December 1, 2000): 1668–77. http://dx.doi.org/10.1104/pp.124.4.1668.

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Journal articles on the topic 'FTSJ1'

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