Relevant bibliographies by topics / C-terminal domain of perlecan

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Academic literature on the topic 'C-terminal domain of perlecan'

Author: Grafiati
Published: 11 March 2023

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Journal articles on the topic "C-terminal domain of perlecan"

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Zoeller, Jason J., Angela McQuillan, John Whitelock, Shiu-Ying Ho, and Renato V. Iozzo. "A central function for perlecan in skeletal muscle and cardiovascular development." Journal of Cell Biology 181, no. 2 (April 21, 2008): 381–94. http://dx.doi.org/10.1083/jcb.200708022.

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Perlecan's developmental functions are difficult to dissect in placental animals because perlecan disruption is embryonic lethal. In contrast to mammals, cardiovascular function is not essential for early zebrafish development because the embryos obtain adequate oxygen by diffusion. In this study, we use targeted protein depletion coupled with protein-based rescue experiments to investigate the involvement of perlecan and its C-terminal domain V/endorepellin in zebrafish development. The perlecan morphants show a severe myopathy characterized by abnormal actin filament orientation and disorganized sarcomeres, suggesting an involvement of perlecan in myopathies. In the perlecan morphants, primary intersegmental vessel sprouts, which develop through angiogenesis, fail to extend and show reduced protrusive activity. Live videomicroscopy confirms the abnormal swimming pattern caused by the myopathy and anomalous head and trunk vessel circulation. The phenotype is partially rescued by microinjection of human perlecan or endorepellin. These findings indicate that perlecan is essential for the integrity of somitic muscle and developmental angiogenesis and that endorepellin mediates most of these biological activities.
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Nakamura, Kuniyuki, Tomoko Ikeuchi, Kazuki Nara, Craig S. Rhodes, Peipei Zhang, Yuta Chiba, Saiko Kazuno, et al. "Perlecan regulates pericyte dynamics in the maintenance and repair of the blood–brain barrier." Journal of Cell Biology 218, no. 10 (September 20, 2019): 3506–25. http://dx.doi.org/10.1083/jcb.201807178.

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Ischemic stroke causes blood–brain barrier (BBB) breakdown due to significant damage to the integrity of BBB components. Recent studies have highlighted the importance of pericytes in the repair process of BBB functions triggered by PDGFRβ up-regulation. Here, we show that perlecan, a major heparan sulfate proteoglycan of basement membranes, aids in BBB maintenance and repair through pericyte interactions. Using a transient middle cerebral artery occlusion model, we found larger infarct volumes and more BBB leakage in conditional perlecan (Hspg2)-deficient (Hspg2−/−-TG) mice than in control mice. Control mice showed increased numbers of pericytes in the ischemic lesion, whereas Hspg2−/−-TG mice did not. At the mechanistic level, pericytes attached to recombinant perlecan C-terminal domain V (perlecan DV, endorepellin). Perlecan DV enhanced the PDGF-BB–induced phosphorylation of PDGFRβ, SHP-2, and FAK partially through integrin α5β1 and promoted pericyte migration. Perlecan therefore appears to regulate pericyte recruitment through the cooperative functioning of PDGFRβ and integrin α5β1 to support BBB maintenance and repair following ischemic stroke.
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Miosge, Nicolai, Timo Simniok, Patricia Sprysch, and Rainer Herken. "The Collagen Type XVIII Endostatin Domain Is Co-localized with Perlecan in Basement Membranes in Vivo." Journal of Histochemistry & Cytochemistry 51, no. 3 (March 2003): 285–96. http://dx.doi.org/10.1177/002215540305100303.

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The C-terminal globular endostatin domain of collagen type XVIII is anti-angiogenic in a variety of experimental tumor models, and clinical trials to test it as an anti-tumor agent are already under way. In contrast, many of its cell biological properties are still unknown. We systematically localized the mRNA of collagen type XVIII with the help of in situ hybridization (ISH) and detected it in epithelial and mesenchymal cells of almost all organ systems throughout mouse development. Light and electron microscopic immunohistochemistry (IHC) revealed that the endostatin domain is a widespread component of almost all epithelial basement membranes in all major developing organs, and in all basement membranes of capillaries and blood vessels. Furthermore, quantitative immunogold double labeling demonstrated a co-localization of 50% of the detected endostatin domain together with perlecan in basement membranes in vivo. We conclude that the endostatin domain of collagen type XVIII plays a role, even in early stages of mouse development, other than regulating angiogenesis. In the adult, the endostatin domain could well be involved in connecting collagen type XVIII to the basement membrane scaffolds. At least in part, perlecan appears to be an adaptor molecule for the endostatin domain in basement membranes in vivo.
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Mullen, Gregory P., Teresa M. Rogalski, Jason A. Bush, Poupak Rahmani Gorji, and Donald G. Moerman. "Complex Patterns of Alternative Splicing Mediate the Spatial and Temporal Distribution of Perlecan/UNC-52 in Caenorhabditis elegans." Molecular Biology of the Cell 10, no. 10 (October 1999): 3205–21. http://dx.doi.org/10.1091/mbc.10.10.3205.

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The unc-52 gene encodes the nematode homologue of mammalian perlecan, the major heparan sulfate proteoglycan of the extracellular matrix. This is a large complex protein with regions similar to low-density lipoprotein receptors, laminin, and neural cell adhesion molecules (NCAMs). In this study, we extend our earlier work and demonstrate that a number of complex isoforms of this protein are expressed through alternative splicing. We identified three major classes of perlecan isoforms: a short form lacking the NCAM region and the C-terminal agrin-like region; a medium form containing the NCAM region, but still lacking the agrin-like region; and a newly identified long form that contains all five domains present in mammalian perlecan. Using region-specific antibodies andunc-52 mutants, we reveal a complex spatial and temporal expression pattern for these UNC-52 isoforms. As well, using a series of mutations affecting different regions and thus different isoforms of UNC-52, we demonstrate that the medium NCAM-containing isoforms are sufficient for myofilament lattice assembly in developing nematode body-wall muscle. Neither short isoforms nor isoforms containing the C-terminal agrin-like region are essential for sarcomere assembly or muscle cell attachment, and their role in development remains unclear.
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Chung, C. Y., and H. P. Erickson. "Glycosaminoglycans modulate fibronectin matrix assembly and are essential for matrix incorporation of tenascin-C." Journal of Cell Science 110, no. 12 (June 15, 1997): 1413–19. http://dx.doi.org/10.1242/jcs.110.12.1413.

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We have investigated the role of glycosaminoglycans in fibronectin matrix assembly and the incorporation of tenascin-C into matrix fibrils. Chinese hamster ovary cell mutants with a total block in heparan and chondroitin sulfate production failed to assemble a fibronectin matrix, and incorporated no tenascin-C. Another mutant with reduced heparan sulfate produced a normal fibronectin matrix but failed to incorporate tenascin-C. Excess soluble glycosaminoglycans inhibited the binding of tenascin-C to purified fibronectin in ELISA, and completely blocked incorporation into matrix fibrils. Treating cultured cells with xyloside, which interferes with glycosaminoglycan attachment to proteoglycans, also completely blocked their ability to incorporate tenascin-C into matrix fibrils. We conclude that proteoglycans bound to fibronectin fibrils play a major role in binding tenascin-C to these fibrils. We examined more closely the large heparan sulfate proteoglycan, perlecan, and found that it co-localizes with tenascin-C and fibronectin in the matrix. The perlecan binding site in tenascin-C was mapped to the fibronectin type III domains 3–5, but this binding was strongly enhanced for the small splice variant, which is the major form incorporated into the matrix. Apparently when the alternative splice segment is inserted after domain 5 it inhibits perlecan binding. Thus heparan sulfate glycosaminoglycans, and perlecan in particular, may play a role in incorporation of the small splice variant of tenascin-C into fibronectin matrix fibrils.
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Bix, Gregory, Jian Fu, Eva M. Gonzalez, Laura Macro, Amy Barker, Shelly Campbell, Mary M. Zutter, et al. "Endorepellin causes endothelial cell disassembly of actin cytoskeleton and focal adhesions through α2β1 integrin." Journal of Cell Biology 166, no. 1 (July 5, 2004): 97–109. http://dx.doi.org/10.1083/jcb.200401150.

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Endorepellin, the COOH-terminal domain of the heparan sulfate proteoglycan perlecan, inhibits several aspects of angiogenesis. We provide evidence for a novel biological axis that links a soluble fragment of perlecan protein core to the major cell surface receptor for collagen I, α2β1 integrin, and provide an initial investigation of the intracellular signaling events that lead to endorepellin antiangiogenic activity. The interaction between endorepellin and α2β1 integrin triggers a unique signaling pathway that causes an increase in the second messenger cAMP; activation of two proximal kinases, protein kinase A and focal adhesion kinase; transient activation of p38 mitogen-activated protein kinase and heat shock protein 27, followed by a rapid down-regulation of the latter two proteins; and ultimately disassembly of actin stress fibers and focal adhesions. The end result is a profound block of endothelial cell migration and angiogenesis. Because perlecan is present in both endothelial and smooth muscle cell basement membranes, proteolytic activity during the initial stages of angiogenesis could liberate antiangiogenic fragments from blood vessels' walls, including endorepellin.
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Hayashi, K., J. A. Madri, and P. D. Yurchenco. "Endothelial cells interact with the core protein of basement membrane perlecan through beta 1 and beta 3 integrins: an adhesion modulated by glycosaminoglycan." Journal of Cell Biology 119, no. 4 (November 15, 1992): 945–59. http://dx.doi.org/10.1083/jcb.119.4.945.

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Aortic endothelial cells adhere to the core protein of murine perlecan, a heparan sulfate proteoglycan present in endothelial basement membrane. We found that cell adhesion was partially inhibited by beta 1 integrin-specific mAb and almost completely blocked by a mixture of beta 1 and alpha v beta 3 antibodies. Furthermore, adhesion was partially inhibited by a synthetic peptide containing the perlecan domain III sequence LPASFRGDKVTSY (c-RGD) as well as by GRGDSP, but not by GRGESP. Both antibodies contributed to the inhibition of cell adhesion to immobilized c-RGD whereas only beta 1-specific antibody blocked residual cell adhesion to proteoglycan core in the presence of maximally inhibiting concentrations of soluble RGD peptide. A fraction of endothelial surface-labeled detergent lysate bound to a core affinity column and 147-, 116-, and 85-kD proteins were eluted with NaCl and EDTA. Polyclonal anti-beta 1 and anti-beta 3 integrin antibodies immunoprecipitated 116/147 and 85/147 kD surface-labeled complexes, respectively. Cell adhesion to perlecan was low compared to perlecan core, and cell adhesion to core, but not to immobilized c-RGD, was selectively inhibited by soluble heparin and heparan sulfates. This inhibition by heparin was also observed with laminin and fibronectin and, in the case of perlecan, was found to be independent of heparin binding to substrate. These data support the hypothesis that endothelial cells interact with the core protein of perlecan through beta 1 and beta 3 integrins, that this binding is partially RGD-independent, and that this interaction is selectively sensitive to a cell-mediated effect of heparin/heparan sulfates which may act as regulatory ligands.
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French, Margaret M., Ronald R. Gomes, Rupert Timpl, Magnus Höök, Kirk Czymmek, Mary C. Farach-Carson, and Daniel D. Carson. "Chondrogenic Activity of the Heparan Sulfate Proteoglycan Perlecan Maps to the N-terminal Domain I." Journal of Bone and Mineral Research 17, no. 1 (January 1, 2002): 48–55. http://dx.doi.org/10.1359/jbmr.2002.17.1.48.

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Nyström, Alexander, Zabeena P. Shaik, Donald Gullberg, Thomas Krieg, Beate Eckes, Roy Zent, Ambra Pozzi, and Renato V. Iozzo. "Role of tyrosine phosphatase SHP-1 in the mechanism of endorepellin angiostatic activity." Blood 114, no. 23 (November 26, 2009): 4897–906. http://dx.doi.org/10.1182/blood-2009-02-207134.

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Abstract Endorepellin, the C-terminal domain of perlecan, is a powerful angiogenesis inhibitor. To dissect the mechanism of endorepellin-mediated endothelial silencing, we used an antibody array against multiple tyrosine kinase receptors. Endorepellin caused a widespread reduction in phosphorylation of key receptors involved in angiogenesis and a concurrent increase in phosphatase activity in endothelial cells and tumor xenografts. These effects were efficiently hampered by function-blocking antibodies against integrin α2β1, the functional endorepellin receptor. The Src homology-2 protein phosphatase-1 (SHP-1) coprecipitated with integrin α2 and was phosphorylated in a dynamic fashion after endorepellin stimulation. Genetic evidence was provided by lack of an endorepellin-evoked phosphatase response in microvascular endothelial cells derived from integrin α2β1−/− mice and by response to endorepellin in cells genetically engineered to express the α2β1 integrin, but not in cells either lacking this receptor or expressing a chimera harboring the integrin α2 ectodomain fused to the α1 intracellular domain. siRNA-mediated knockdown of integrin α2 caused a dose-dependent reduction of SHP-1. Finally, the levels of SHP-1 and its enzymatic activity were substantially reduced in multiple organs from α2β1−/− mice. Our results show that SHP-1 is an essential mediator of endorepellin activity and discover a novel functional interaction between the integrin α2 subunit and SHP-1.
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GARBE, Jörg H. O., Walter GÖHRING, Karlheinz MANN, Rupert TIMPL, and Takako SASAKI. "Complete sequence, recombinant analysis and binding to laminins and sulphated ligands of the N-terminal domains of laminin α3B and α5 chains." Biochemical Journal 362, no. 2 (February 22, 2002): 213–21. http://dx.doi.org/10.1042/bj3620213.

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The N-terminal sequences of mouse laminin α3B and α5 chains have been completed and demonstrate the presence of a signal peptide followed by a complete laminin N-terminal (LN) module (domain VI). These signal peptides were released after recombinant production of larger fragments comprising domains VI/V (45–65kDa) from this region yielding properly folded proteins, which were secreted from HEK-293—EBNA cells. Pepsin digestion of these fragments yielded products of 25–35kDa, which consisted only of domain V. The αVI/V fragments were able to inhibit self-assembly of laminin-1, with those from the α3B and α5 chains being more active than those from α1 and α2 chains. Domain V fragments, however, showed a reduced activity, indicating the major contribution of the LN module in inhibition. These interactions were confirmed by surface-plasmon-resonance assays demonstrating moderate affinities (Kd = 0.02 to > 6μM) for the binding to laminin-1. This indicated that laminins containing α3B or α5 chains should also be able to form non-covalent networks by polymerization. The LN modules also showed heparin binding in affinity chromatography, which was strongest for α1/α2, moderate for α3B, whereas no binding was observed for α5. They all bound to heparan sulphate chains of perlecan and to sulphatides, with a lower variability in binding activity. Specific antibodies were raised against α3BVI/V and α5VI/V and were shown to stain basement membrane zones in various mouse tissues. These antibodies also allowed the identification of a new laminin assembly form 5B consisting of α3B, β3 and γ2 chains.
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Dissertations / Theses on the topic "C-terminal domain of perlecan"

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Guo, Xiangxue. "Biochemical and Bioinformatics Analysis of CVAB C-Terminal Domain." Digital Archive @ GSU, 2006. http://digitalarchive.gsu.edu/biology_diss/3.

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Cytoplasmic membrane proteins CvaB and CvaA and the outer membrane protein TolC form the bacteriocin colicin V (ColV) secretion system in Escherichia coli. CvaB functions as an ATP-binding cassette transporter with nucleotide-binding motifs in the C-terminal domain (CTD). To study the role of CvaB-CTD in the ColV secretion, a truncated construct of this domain was made and over-expressed. Different forms of CvaB-CTD were obtained during purification, and were identified as monomer, dimer, and oligomer on gel filtration. Nucleotide binding was shown critical for the CvaB-CTD dimerization: oligomers could be converted into dimers by nucleotide bindings; the removal of nucleotide from dimers resulted in transient monomers followed by CTD oligomerization and aggregation; no dimer form could be cross-linked from the nucleotide-binding deficient mutant D654H. The spatial proximity of the Walker A site and ABC signature motif in CTD dimer was identified through disulfide cross-linking of mixed CvaB-CTD with mutants A530C and L630C, while mutations did not dimerize individually. Those results indicated that the CvaB-CTD formed a nucleotide-dependent head-to-tail dimer. Molecular basis of differential nucleotide bindings was also studied through bioinformatics prediction and biochemical verification. Through sequence alignment and homology modeling with bound ATP or GTP, it was found that the Ser503 and Gln504 on aromatic stacking region (Y501DSQ-loop) of CvaB-CTD provided two additional hydrogen-bonds to GTP, but not to ATP. Site-directed mutations of the S503A and/or Q504L were designed based on the model. While site-directed mutagenesis studies of Walker A&B sites or the ABC signature motif affected little on the GTP-binding preference, the double mutation (S503A/Q504L) on the Y501DSQ-loop increased both ATP-binding and ATPase activity at low temperatures. The double mutant showed slight decrease of GTP-binding and about 10-fold increase of the ATP/GTP-binding ratio. Similar temperature sensitivity in nucleotide-binding and activity assays were identified in the double mutant at the same time. Mutations on the Y501DSQ-loop did not affect the ColV secretion level in vivo. Together, the Y501DSQ-loop is structurally involved in the differential binding of GTP over ATP.
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Carvalho, Maria João Marques de. "Characterization of a C-terminal domain from eag potassium channel." Master's thesis, Universidade de Aveiro, 2010. http://hdl.handle.net/10773/4343.

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Mestrado em Métodos Biomoleculares
Domínios que ligam nucleotideos cíclicos (CNBD) regulam muitas vias de sinalização em células procarióticas e eucarióticas. Os ligandos AMP cíclico ou GMP cíclico ligam-se a estes domínios e induzem uma alteração conformacional que é propagada ao domínio efector, como uma cinase ou um canal iónico. Os canais de potássio da família ether-a-go-go (EAG) estão envolvidos em muitos processos fisiológicos que incluem repolarização cardíaca e neuronal, proliferação tumoral e secreção de hormonas. Estes canais são tetraméricos e cada subunidade inclui seis hélices transmembranares e dominios citoplasmáticos em N- e C-terminal. O domínio em C-terminal tem homologia com domínios que ligam nucleotídeos cíclicos mas foi demonstrado que os canais EAG não são afectados por nucleotídeos e o domínio não liga nucleotideos. O objectivo deste projecto foi resolver a estrutura de um domínio C-terminal de um canal EAG por cristalografia de raios-X e compreender o seu papel funcional. Determinei a estrutura de um destes domínios à resolução de 2,2 Å; a estrutura tem a topologia de um CNBD mas a cavidade de ligação apresenta várias diferenças relativamente à de domínios que ligam nucleotideos cíclicos. Mais ainda, os canais EAG são inibidos por calmodulina e há dois locais de ligação de calmodulina a seguir ao CNBD. A estrutura mostrou que um destes locais se encontra sobreposto com uma região do domínio levantando a possibilidade da calmodulina regular o canal através da alteração conformacional do domínio C-terminal dos canais EAG. Esta possibilidade começou a ser explorada com recurso a ensaios de cross-linking químico e espectroscopia de fluorescência.
Cyclic nucleotide binding domains (CNBD) are regulatory domains that participate in many signaling pathways in prokaryotic and eukaryotic cells. The ligand cAMP or cGMP binds these domains and induces a conformational change that is propagated to an effector domain, like a kinase or an ion channel. The ether-a-go-go (EAG) potassium channel family is involved in important physiological roles that include cardiac and neuronal repolarization, tumor proliferation and hormone secretion. These channels are tetramers, where each subunit includes six transmembrane helices and N- and C-terminal cytoplasmic domains. The C-terminal domain has strong homology to CNBDs but it has been demonstrated that EAG channels are not affected by cyclic nucleotides and that the domain does not bind nucleotides. The ultimate goal of this project was to solve the structure of an EAG family C-terminal domain by X-ray crystallography and to understand its functional role. I have determined the structure of one of these domains at 2.2 Å; the structure has the canonical CNBD fold but it shows a ligand pocket that has several differences relative to a cyclic nucleotide binding site. Furthermore, EAG currents are inhibited by calmodulin binding and there are two calmodulin binding sites C-terminal to the CNBD. The structure reveals that one of these sites overlaps with a region of the domain raising the possibility that calmodulin affects channel function by changing the EAG C-terminal domain conformation. I have conducted preliminary tests on this hypothesis by using biochemical cross-linking experiments and fluorescence spectroscopy.
FCT
FCOMP-010124-FEDER-007427/PTDC/QUI/66171/2006
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Miller, Wayne. "Structural characterisation of the prokaryotic sodium channel C-terminal domain." Thesis, Birkbeck (University of London), 2015. http://bbktheses.da.ulcc.ac.uk/140/.

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Since the discovery of the first prokaryotic voltage gated sodium channel (Nav) in 2001, prokaryotic Navs have been a high priority target for structural study. Prokaryotic Navs are of interest as a model system due to their homology to eukaryotic Navs, which are high value drug development targets for their roles in pain perception and neural function. While prokaryotic Navs have function and pharmacology distinct from their eukaryotic homologues, understanding their structure holds implications for drug development and for understanding diseases stemming from neuronal dysfunction. However, Navs have historically been challenging targets for structural study, resisting attempts at crystallisation until recently. In this study, expression, purification, and characterisation of a chimera of the NavBh channel and the ligand gating RCK domain from the prokaryotic potassium channel MthK has been performed. It was hypothesised that the addition of the RCK domain would improve the channel’s crystallisation potential, and create a ligand gated Nav for functional characterisation. Electrophysiological studies demonstrated that the RCK domain was capable of gating NavBh, however the chimera had reduced solubility, indicating that this chimeric fusion was not an ideal target for structural study due to low purification yields. Following this, and in light of recent studies that suggested the structure of the prokaryotic Nav C-terminus had a role in channel function, structural analysis of the C-terminus of a prokaryotic Nav homologue cloned from Bacillus alcalophilus has been performed. Synchrotron radiation circular dichroism analysis of serial C-terminal truncations demonstrated the structure of the NsvBa C-terminus consists of a helical region connected to the channel pore by a disordered neck region, despite conflicting bioinformatics predictions. This offers further support for the hypothesis that in functional Navs, the C-terminus consists of a disordered neck region connecting a coiled-coil to the base of the pore, which acts as a spring to assist in channel gating and inactivation.
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Benetti, Federico. "Structural studies on the C-terminal domain of human PMCA1b." Doctoral thesis, Università degli studi di Padova, 2008. http://hdl.handle.net/11577/3425143.

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Plasma Membrane Calcium ATPases (PMCAs) are P-type pumps involved in calcium homeostasis. Their 3D structures are still unknown but a possible topology has been predicted. PMCAs are predicted to have a cytosolic N-terminal domain, a cytosolic C-terminal domain (regulatory domain), ten transmembrane segments and two cytosolic loops called transduction domain and catalytic domain that connect the 2nd and the 3rd, the 4th and the 5th transmembrane segments respectively. Several mechanisms are responsible of their activation: interaction with Ca2+-calmodulin, interaction with acidic phospholipids and fatty acids, phosphorylation with kinases A and C, proteolysis by calpain and oligomerization. All activation mechanisms decrease the Km values, in particular the oligomerization brings this value around at the value of cytosolic calcium concentration present in the resting cells (50-100 nM). The C-terminal domain is a structural motif that distinguishes PMCAs from all other P-type pumps. It is also the target of all activators and activation mechanisms. In this study we have described the secondary structure and tertiary structure at low resolution of the C-terminal regulatory domain of the human PMCA isoform 1b. We have found that the domain forms aggregates by intermolecular interactions. Moreover, we have studied the reversibility of the oligomerization process and found the best conditions to stabilize the C-terminal domain in the monomeric form. These conditions imply the presence of the lipid mimetic SDS at critical micellar concentration. A structural reconstruction based on Small Angle Neutron Scattering experiments provides a low resolution structure where the C-terminal domain has an hourglass shape. The central cross section compatible with that of an ?-helix. This part could correspond at the ?-helix of the C28W calmodulin binding region while the downstream and upstream regions could be random coil as also predicted by PSIpred. Binding experiments between the C-terminal domain and the Ca2+- calmodulin have been carried out. The aim was to study whether in a phospholipid mimetic system necessary to stabilize the monomeric form, such as sodium dodecyl sulphate, this domain can still interact with calmodulin. The phospholipid mimetic system that stabilize the domain in the monomeric form prevent its binding with Ca2+-calmodulin. The results suggest that a different aggregation state of the PMCAs exist in diverse membrane rafts: membrane rafts rich in uncharged or zwitterionic phospholipids could contain PMCAs in oligomeric form while membrane rafts rich in acidic phospholipids could contain PMCAs in monomeric form.
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Adu-Bobie, Jeanette. "Characterisation of the C-terminal domain intimin from enteropathogenic Escherichia coli." Thesis, Imperial College London, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.300436.

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Ragan, Timothy James. "Regulation of S6K1 Protein Kinae Activation by its C-Terminal Autoinhibitory Domain." Scholarly Repository, 2008. http://scholarlyrepository.miami.edu/oa_dissertations/125.

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Signal transduction kinases lie at the heart of the cell's ability to respond to environmental cues. These kinases are typically controlled by post-translational modification, most commonly by phosphorylation. S6K1alphaII is a member of the AGC subfamily of serine-threonine protein kinases, whereby catalytic activation requires phosphorylation of critical residues in the conserved T-loop (T229) and hydrophobic motif (T389) regions of its catalytic kinase domain. In addition to its kinase domain, S6K1 contains a C-terminal autoinhibitory domain (AID, residues 399-502), which inhibits T-loop and hydrophobic motif phosphorylation. Autoinhibition is relieved upon multi-site Ser-Thr phosphorylation of the AID by MAP kinase(s). We developed an optimized PCR-based gene synthesis method, which I utilized to build expression constructs for the AID alone as well as the kinase domain and full length S6K1alphaII. A fully activated form of S6K1alphaII was purified from Sf9 cells by co-expression with PDK1, and was used for in vitro analysis of the signaling pathway. AID was successfully purified in a soluble form from E. coli despite the fact that PONDR analysis predicted a highly disordered structure. Aberrant mobilities in both SDS-PAGE and size-exclusion chromatography, as well as low chemical shift dispersion in 1H-15N HSQC spectra and far UV CD data showing a lack of secondary structure, confirmed that purified recombinant AID is largely unfolded. Despite this, addition of purified AID effectively inhibited PDK1-catalyzed T-loop phosphorylation of a catalytic kinase domain construct of S6K1 and inhibition was decreased when the tetraphospho-mimic mutant AID(D2ED) was used. These studies, along with the reagents produced by them, will allow for further exploration of the emerging field of disordered regulatory domains.
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Panagiotidou, P. "Cloning, expression and structural studies on the C-terminal domain of procollagen C-proteinase enhancer (ctPCPE)." Thesis, University of Kent, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.405998.

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Al-Ali, Hassan. "Regulation of PDK1 Protein Kinase Activation by Its C-Terminal Pleckstrin Homology Domain." Scholarly Repository, 2010. http://scholarlyrepository.miami.edu/oa_dissertations/381.

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Phosphoinositide-dependent protein kinase-1 (PDK1) plays an integral role in signaling cellular growth and proliferation, one that's dependent on its ability to autophosphorylate Ser-241 in its T-loop. This process appears to have a strict requirement for its C-terminal pleckstrin homology (PH) domain. Thus, the overall objective of this work was to determine the mechanism by which the PH domain induces an active kinase conformation in unphosphorylated PDK1, capable of Ser-241 autophosphorylation. First, computational modeling and protein cross linking studies were combined with site-directed mutagenesis and kinetic assays in order to provide initial assessment of how the PH domain scaffolds Ser-241 autophosphorylation. A significant number of contacts were identified between the enigmatic "N-bud" region of the PH domain and the kinase domain. Specifically, these studies implicated Glu-432 and Glu-453 of the N-bud region of the PH domain that bind and serve as mimics of the phosphorylated Ser-241 in the T-loop and the phosphorylated C-terminal tail of PDK1 substrates, respectively. Next, a novel method for protein trans-splicing of the regulatory and catalytic kinase domains of PDK1 was developed. The method utilizes the N- and C-terminal split inteins of the gene dnaE from Nostoc punctiforme [(N)NpuDnaE] and Synechocystis sp. strain PCC6803 [(C)SspDnaE], respectively. The cross-reacting KINASE(AEY)-(N)NpuDnaE-His6 and GST-His6-(C)SspDnaE-(CMN)PH fusion constructs generated full length spliced-PDK1 with kobs = (2.8 +- 0.3) x 10-5 s-1. Finally, NMR was used to further characterize the structural and dynamical properties of the PH domain in both its isolated form and in full length PDK1. Whereas, it was not possible to obtain chemical shift assignments of any backbone or side chain nuclear resonances, methods were optimized for 2H,13C,15N-isotopic labeling of the recombinant PH domain. Furthermore, the protein trans-splicing method was significantly improved and utilized for segmental isotopic labeling of the PH domain in full length PDK1. These new findings and developments may provide specific insight and technological improvements towards future studies aimed to better understand and target autoinhibited conformations of PDK1 for translational purposes.
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Chapman, Rob. "A Functional Analysis of the RNA Polymerase II Large Subunit C-Terminal Domain." Diss., lmu, 2003. http://nbn-resolving.de/urn:nbn:de:bvb:19-11049.

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Ray, Pampa. "DNA binding studies of the transcriptional activator NifA and its c-terminal domain." Thesis, University of Birmingham, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.393779.

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Books on the topic "C-terminal domain of perlecan"

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Ray, Pampa. DNA binding studies of the transcriptional activator NifA and its C-terminal domain. Birmingham: University of Birmingham, 2000.

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Yurko, Nathan Michael. The roles of Threonine-4 and Tyrosine-1 of the RNA Polymerase II C-Terminal Domain: New insights into transcription from Saccharomyces cerevisiae. [New York, N.Y.?]: [publisher not identified], 2017.

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Book chapters on the topic "C-terminal domain of perlecan"

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Southan, Christopher, Elizabeth Thompson, and David A. Lane. "The C-terminal polymerisation domain of fibrinogen." In Fibrin formation and Fibrinolysis, edited by D. A. Lane, 47–54. Berlin, Boston: De Gruyter, 1986. http://dx.doi.org/10.1515/9783110871951-007.

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Libich, David S., Samjhana Pandey, and Steven M. Pascal. "Conformational Studies of the Par-4 C-Terminal Domain." In Tumor Suppressor Par-4, 95–126. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-73572-2_3.

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Hoffmann, Ralf, Randall E. Bolger, Zhi Quan Xiang, Magdalena Blaszczyk-Thurin, Hildegund C. J. Ertl, and Laszlo Otvos. "Phosphopeptide models of the C-terminal basic domain of p53." In Peptides Frontiers of Peptide Science, 715–16. Dordrecht: Springer Netherlands, 2002. http://dx.doi.org/10.1007/0-306-46862-x_313.

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KOIWA, HISASHI. "Phosphorylation of RNA polymerase II C-terminal domain and plant osmotic-stress responses." In Abiotic stress tolerance in plants, 47–57. Dordrecht: Springer Netherlands, 2006. http://dx.doi.org/10.1007/1-4020-4389-9_3.

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Yumoto, Fumiaki, Koji Nagata, Kyoko Adachi, Nobuaki Nemoto, Takao Ojima, Kiyoyoshi Nishita, Iwao Ohtsuki, and Masaru Tanokura. "NMR Structural Study of Troponin C C-Terminal Domain Complexed with Troponin I Fragment from Akazara Scallop." In Advances in Experimental Medicine and Biology, 195–201. Boston, MA: Springer US, 2003. http://dx.doi.org/10.1007/978-1-4419-9029-7_18.

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Takagi, Takashi. "Amino Acid Sequence of the C-Terminal Domain of Octopus (Paroctopus dofleini dofleini) Hemocyanin." In Invertebrate Oxygen Carriers, 259–62. Berlin, Heidelberg: Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71481-8_46.

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Hatakeyama, Tomomitsu, Tomoko Suenaga, Takuro Niidome, and Haruhiko Aoyagi. "Antibacterial Peptides Derived from the C-Terminal Domain of the Hemolytic Lectin, CEL-III." In Peptides: The Wave of the Future, 760–61. Dordrecht: Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-010-0464-0_355.

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Kang, Mona E., and Michael E. Dahmus. "The Unique C-Terminal Domain of RNA Polymerase II and Its Role in Transcription." In Advances in Enzymology - and Related Areas of Molecular Biology, 41–77. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470123171.ch2.

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Jiménez, M. A., M. Bruix, J. L. Nieto, and M. Rico. "1H NMR study on the folding of peptide fragments from the thermolysin C-terminal domain." In Peptides 1990, 531–32. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3034-9_223.

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Cooper, Christopher D. O., and Brian D. Marsden. "N- and C-Terminal Truncations to Enhance Protein Solubility and Crystallization: Predicting Protein Domain Boundaries with Bioinformatics Tools." In Methods in Molecular Biology, 11–31. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6887-9_2.

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Conference papers on the topic "C-terminal domain of perlecan"

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AYABE, K., T. ZAKO, and H. UEDA. "IMPORTANCE OF FIREFLY LUCIFERASE C-TERMINAL DOMAIN IN BINDING OF LUCIFERYL-ADENYLATE." In Proceedings of the 13th International Symposium. WORLD SCIENTIFIC, 2005. http://dx.doi.org/10.1142/9789812702203_0010.

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Beneckv, M. J., C. G. Kolvenbach, D. L. Amrani, and M. W. Mosesson. "EVIDENCE THAT THE C-TERMINAL HEPARIN BINDING DOMAIN ("HEP II") DOMINATES HEPARIN-FIBRONECTIN INTERACTIONS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643631.

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The interaction of glycosaminoglycans with plasma fibronectin (PFn) may play a role in the conversion of PFn from an “inert” dimeric circulating form to an “activated” multimeric form deposited on the cell surface or in the extracellular matrix. We carried out a quantitative comparison of heparin affinity for PFn and its proteolytic fragments in order to assess the relative importance of heparin interactions with PFn’s various reported heparin-binding domains. We employed affinity chromatography on PFn-sepharose to prepare a subset of fluorescein-labelled heparin molecules with high affinity for PFn, and confirmed that heparin binding to PFn is very sensitive to ionic strength. This suggests that the PFn-sepharose column selectively binds a fraction of highly sulfated heparin molecules. We quantified PFn-heparin affinity in the fluid-phase by monitoring a fluorescence polarization change that occurred as a consequence of the decrease in the rotational diffusion rate of fluorescently-labelled heparin molecules (13.8 kD) as they became “immobilized” by binding to PFn. Scatchard analysis of the heparin fluorescence polarization data obtained for PFn in Tris-buffered saline yielded a biphasic curve with Kd’s estimated at 5 and 130 nM, respectively A 190 kD thrombin fragment, containing the C-terminal "Hep II" domain but lacking the 29 kD N-terminal “Hep I” domain, yielded a linear plot displaying a single class of heparin-binding sites with a Kd of 130 nM Similar results were obtained for the C-terminal 150 kD Fn fragment which also contained the “Hep II” domain. In contrast, the 29 kD N-terminal “Hep I” Fn fragment bound heparin weakly (Kd =25 μM). The nature of the “high affinity (Kd= 5 nM) heparin binding component is uncertain; it may reflect heparin interaction with soluble multimers present in our PFn preparations Our observations suggest that the Kd=130 nM heparin binding component corresponds to heparin interaction with the C-terminal “Hep II” domain We conclude that the N-terminal “Hep I” domain does not participate significantly in heparin binding to soluble dimeric Fn under physiological conditions, whereas the C-terminal “Hep II” domain dominates such interactions
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Boohaker, Rebecca, Ge Zhang, Kathleen Nemec, and Annette R. Khaled. "Abstract 2010: Development of a cytotoxic peptide based on the C-terminal domain of Bax." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-2010.

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Caballero-Ruiz, Begoña, Cintli C. Morales-Alcala, Henry M. Wood, Gianluca Canettieri, and Natalia A. Riobo-Del Galdo. "Abstract 2421: PTCH1 C-terminal domain truncations in colorectal cancer increase mitogenic signalling and autophagy." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-2421.

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Lundine, Devon, Zafar Syed, Viola Ellison, George Annor, Gu Xiao, and Jill Bargonetti. "Abstract 2410: The mutant p53 C-terminal domain assists in DNA interactions and cell cycle promotion." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-2410.

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Iwamoto, M., N. Sugiyama, T. Sasaki, and Y. Abiko. "DOMAIN OF BINDING ACTIVITY WITH PLASMIN KRINGLE IN SYNTHESIZED C-TERMINAL PEPTIDES , OF α2-PLASMIN INHIBITOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644612.

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The inhibitory reaction between plasmin and α2-plasmin inhibitor (α2-PI) proceeds with two steps, a very fast reversible reaction followed by a slower irreversible transition. The first step is dependent on the interaction between lysine binding site (LBS) of plasmin and the corresponding complementary site of α2-PI (kringle binding site(KBS)). It has been reported that KBS is located in a C-terminal tryptic fragment (T-11; J. Biochem. 99, 1699 (1986)).In order to investigate which amino acid residues of T-ll play important roles in binding of plasmin kringle, we tested inhibitory activity of synthesized peptides on the apparent rate constant in the reaction between α2-PI and plasmin. 50% inhibition concentrations of T-ll, peptide I, II, III and IV were 7, 18, 13, 35 and 250pM respectively, indicating that Leu9-Lysl0 is an important part for binding of T-ll to LBS. Peptide III lost its activity by depletion or amidation of the C-terminal lysine residue.In the system consisted of α2-PI and miniplasmin which lacked kringle 1-4, peptide I did not inhibit the interaction between them. Furthermore, peptide II competitively inhibited the binding of tranexamic acid to kringle 1-3 (Ki 0.85μM).These findings suggest that the C-terminal part is involved in the high affinity binding of α2-PI to plasmin kringle and that LyslO in T-ll and C-terminal carboxyl residue play crucial roles in binding to LBS of kringle.
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ZUBAREVA, V. M., D. O. TRETYAKOV, A. S. LAPASHINA, and B. A. FENIOUK. "THE EFFECT OF C-TERMINAL DOMAIN OF SUBUNIT ON ATPASE ACTIVITY OF BACILLUS SUBTILIS ATP SYNTHASE." In HOMO SAPIENS LIBERATUS. TORUS PRESS, 2020. http://dx.doi.org/10.30826/homosapiens-2020-39.

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Golubeva, Volha A., Nicholas T. Woods, and Alvaro N. A. Monteiro. "Abstract 3779: Mutational analysis of MCPH1 C-terminal tandem BRCT domain reveals residues essential for cell cycle arrest." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-3779.

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Robert, Xavier, Richard Haser, Haruhide Mori, Birte Svensson, and Nushin Aghajari. "CARBOHYDRATE RECOGNITION AND SPECIFICITY DIFFERENCES OF BARLEY ALPHA-AMYLASE ISOZYMES: A NOVEL ROLE OF THEIR C-TERMINAL DOMAIN." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.479.

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Lin, Yu-Ching, Li-Ting Lu, Xin-Hua Feng, and Ruey-Hwa Chen. "Abstract 1971: Small C-terminal domain phosphatase 1 stabilizes PML to regulate the progression of renal clear cell carcinoma." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-1971.

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Reports on the topic "C-terminal domain of perlecan"

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Yalovsky, Shaul, and Julian Schroeder. The function of protein farnesylation in early events of ABA signal transduction in stomatal guard cells of Arabidopsis. United States Department of Agriculture, January 2002. http://dx.doi.org/10.32747/2002.7695873.bard.

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Loss of function mutations in the farnesyltransferase β subunit gene ERA1 (enhanced response to abscisic acid), cause abscisic acid hypersensitivity in seedlings and in guard cells. This results in slowed water loss of plants in response to drought. Farnesyltransferase (PFT) catalyses the attachment of the 15-carbon isoprenoid farnesyl to conserved cysteine residues located in a conserved C-terminal domain designated CaaX box. PFT is a heterodimeric protein comprised of an a and b sununits. The a subunit is shared between PFT and geranylgeranyltransferase-I (PGGTI) which catalyses the attachemt of the 20-carbon isoprenoid geranylgeranyl to CaaX box proteins in which the last amino acid is almost always leucine and in addition have a polybasic domain proximal to the CaaL box. Preliminary data presented in the proposal showed that increased cytoplasmic Ca2+ concentration in stomal guard cells in response to non-inductive ABA treatements. The goals set in the proposal were to characterize better how PFT (ERA1) affects ABA induced Ca2+ concentrations in guard cells and to identify putative CaaX box proteins which function as negative regulators of ABA signaling and which function is compromised in era1 mutant plants. To achieve these goals we proposed to use camelion Ca2+ sensor protein, high throughput genomic to identify the guard cell transcriptome and test prenylation of candidate proteins. We also proposed to focus our efforts of RAC small GTPases which are prenylated proteins which function in signaling. Our results show that farnesyltransferaseprenylates protein/s that act between the points of ABA perception and the activation of plasma membrane calcium influx channels. A RAC protein designated AtRAC8/AtRop10 also acts in negative regulation of ABA signaling. However, we discovered that this protein is palmitoylated and not prenylated although it contains a C-terminal CXXX motif. We further discovered a unique C-terminal sequence motif required for membrane targeting of palmitoylatedRACs and showed that their function is prenylation independent. A GC/MS based method for expression in plants, purification and analysis of prenyl group was developed. This method would allow highly reliable identification of prenylated protein. Mutants in the shared α subunit of PFT and PGGT-I was identified and characterized and was shown to be ABA hypersensitive but less than era1. This suggested that PFT and PGGT-I have opposing functions in ABA signaling. Our results enhanced the understanding of the role of protein prenylation in ABA signaling and drought resistance in plants with the implications of developing drought resistant plants. The results of our studies were published 4 papers which acknowledge support from BARD.
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Friedman, Haya, Julia Vrebalov, James Giovannoni, and Edna Pesis. Unravelling the Mode of Action of Ripening-Specific MADS-box Genes for Development of Tools to Improve Banana Fruit Shelf-life and Quality. United States Department of Agriculture, January 2010. http://dx.doi.org/10.32747/2010.7592116.bard.

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Fruit deterioration is a consequence of a genetically-determined fruit ripening and senescence programs, in which developmental factors lead to a climacteric rise of ethylene production in ethylene-sensitive fruits such as tomato and banana. Breeding of tomato with extended fruit shelf life involves the incorporation of a mutation in RIN, a MADS-box transcription factor participating in developmental control signalling of ripening. The RIN mode of action is not fully understood, and it may be predicted to interact with other MADS-box genes to execute its effects. The overall goal of this study was to demonstrate conservation of ripening control functions between banana and tomato and thus, the potential to genetically extend shelf-life in banana based on tools developed in tomato. The specific objectives were: 1. To increase the collection of potential RIN-like genes from banana; 2. To verify their action as developmental regulators; 3. To elucidate MADS-box gene mode of action in ripening control; 4. To create transgenic banana plants that express low levels of endogenous Le-RIN- like, MaMADS- gene(s). We have conducted experiments in banana as well as in tomato. In tomato we have carried out the transformation of the tomato rin mutant with the MaMADS1 and MaMADS2 banana genes. We have also developed a number of domain swap constructs to functionally examine the ripening-specific aspects of the RIN gene. Our results show the RIN-C terminal region is essential for the gene to function in the ripening signalling pathway. We have further explored the tomato genome databases and recovered an additional MADS-box gene necessary for fruit ripening. This gene has been previously termed TAGL1 but has not been functionally characterized in transgenic plants. TAGL1 is induced during ripening and we have shown via RNAi repression that it is necessary for both fleshy fruit expansion and subsequent ripening. In banana we have cloned the full length of six MaMADS box genes from banana and determined their spatial and temporal expression patterns. We have created antibodies to MaMADS2 and initiated ChI assay. We have created four types of transgenic banana plants designed to reduce the levels of two of the MaMADS box genes. Our results show that the MaMADS-box genes expression in banana is dynamically changing after harvest and most of them are induced at the onset of the climacteric peak. Most likely, different MaMADS box genes are active in the pulp and peel and they are differently affected by ethylene. Only the MaMADS2 box gene expression is not affected by ethylene indicating that this gene might act upstream to the ethylene response pathway. The complementation analysis in tomato revealed that neither MaMADS1 nor MaMADS2 complement the rin mutation suggesting that they have functionally diverged sufficiently to not be able to interact in the context of the tomato ripening regulatory machinery. The developmental signalling pathways controlling ripening in banana and tomato are not identical and/or have diverged through evolution. Nevertheless, at least the genes MaMADS1 and MaMADS2 constitute part of the developmental control of ripening in banana, since transgenic banana plants with reduced levels of these genes are delayed in ripening. The detailed effect on peel and pulp, of these transgenic plants is underway. So far, these transgenic bananas can respond to exogenous ethylene, and they seem to ripen normally. The response to ethylene suggest that in banana the developmental pathway of ripening is different than that in tomato, because rin tomatoes do not ripen in response to exogenous ethylene, although they harbor the ethylene response capability This study has a major contribution both in scientific and agricultural aspects. Scientifically, it establishes the role of MaMADS box genes in a different crop-the banana. The developmental ripening pathway in banana is similar, but yet different from that of the model plant tomato and one of the major differences is related to ethylene effect on this pathway in banana. In addition, we have shown that different components of the MaMADS-box genes are employed in peel and pulp. The transgenic banana plants created can help to further study the ripening control in banana. An important and practical outcome of this project is that we have created several banana transgenic plants with fruit of extended shelf life. These bananas clearly demonstrate the potential of MaMADS gene control for extending shelf-life, enhancing fruit quality, increasing yield in export systems and for improving food security in areas where Musaspecies are staple food crops.
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