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Journal articles on the topic 'Cation diffusion facilitators'

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Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

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1

Hudek, L., L. Pearson, A. A. Michalczyk, L. Bräu, B. A. Neilan, and M. L. Ackland. "Characterization of two cation diffusion facilitators NpunF0707 and NpunF1794 in Nostoc punctiforme." Journal of Applied Microbiology 119, no. 5 (September 24, 2015): 1357–70. http://dx.doi.org/10.1111/jam.12942.

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2

Zeytuni, Natalie, René Uebe, Michal Maes, Geula Davidov, Michal Baram, Oliver Raschdorf, Merav Nadav-Tsubery, et al. "Cation Diffusion Facilitators Transport Initiation and Regulation Is Mediated by Cation Induced Conformational Changes of the Cytoplasmic Domain." PLoS ONE 9, no. 3 (March 21, 2014): e92141. http://dx.doi.org/10.1371/journal.pone.0092141.

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3

Anton, Andreas, Annett Weltrowski, Christopher J. Haney, Sylvia Franke, Gregor Grass, Christopher Rensing, and Dietrich H. Nies. "Characteristics of Zinc Transport by Two Bacterial Cation Diffusion Facilitators from Ralstonia metallidurans CH34 and Escherichia coli." Journal of Bacteriology 186, no. 22 (November 15, 2004): 7499–507. http://dx.doi.org/10.1128/jb.186.22.7499-7507.2004.

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ABSTRACT CzcD from Ralstonia metallidurans and ZitB from Escherichia coli are prototypes of bacterial members of the cation diffusion facilitator (CDF) protein family. Expression of the czcD gene in an E. coli mutant strain devoid of zitB and the gene for the zinc-transporting P-type ATPase zntA rendered this strain more zinc resistant and caused decreased accumulation of zinc. CzcD, purified as an amino-terminal streptavidin-tagged protein, bound Zn2+, Co2+, Cu2+, and Ni2+ but not Mg2+, Mn2+, or Cd2+, as shown by metal affinity chromatography. Histidine residues were involved in the binding of 2 to 3 mol of Zn2+ per mol of CzcD. ZitB transported 65Zn2+ in the presence of NADH into everted membrane vesicles with an apparent Km of 1.4 μM and a V max of 0.57 nmol of Zn2+ min−1 mg of protein−1. Conserved amino acyl residues that might be involved in binding and transport of zinc were mutated in CzcD and/or ZitB, and the influence on Zn2+ resistance was studied. Charged or polar amino acyl residues that were located within or adjacent to membrane-spanning regions of the proteins were essential for the full function of the proteins. Probably, these amino acyl residues constituted a pathway required for export of the heavy metal cations or for import of counter-flowing protons.

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4

Cotrim, Camila A., Russell J. Jarrott, Jennifer L. Martin, and David Drew. "A structural overview of the zinc transporters in the cation diffusion facilitator family." Acta Crystallographica Section D Structural Biology 75, no. 4 (April 1, 2019): 357–67. http://dx.doi.org/10.1107/s2059798319003814.

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The cation diffusion facilitators (CDFs) are a family of membrane-bound proteins that maintain cellular homeostasis of essential metal ions. In humans, the zinc-transporter CDF family members (ZnTs) play important roles in zinc homeostasis. They do this by facilitating zinc efflux from the cytoplasm to the extracellular space across the plasma membrane or into intracellular organelles. Several ZnTs have been implicated in human health owing to their association with type 2 diabetes and neurodegenerative diseases. Although the structure determination of CDF family members is not trivial, recent advances in membrane-protein structural biology have resulted in two structures of bacterial YiiPs and several structures of their soluble C-terminal domains. These data reveal new insights into the molecular mechanism of ZnT proteins, suggesting a unique rocking-bundle mechanism that provides alternating access to the metal-binding site.

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5

Keren-Khadmy, Noa, Natalie Zeytuni, Nitzan Kutnowski, Guy Perriere, Caroline Monteil, and Raz Zarivach. "From conservation to structure, studies of magnetosome associated cation diffusion facilitators (CDF) proteins in Proteobacteria." PLOS ONE 15, no. 4 (April 20, 2020): e0231839. http://dx.doi.org/10.1371/journal.pone.0231839.

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6

Li, Liangtao, Ren Miao, Xuan Jia, Diane M. Ward, and Jerry Kaplan. "Expression of the Yeast Cation Diffusion Facilitators Mmt1 and Mmt2 Affects Mitochondrial and Cellular Iron Homeostasis." Journal of Biological Chemistry 289, no. 24 (May 5, 2014): 17132–41. http://dx.doi.org/10.1074/jbc.m114.574723.

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7

Sácký, Jan, Tereza Leonhardt, and Pavel Kotrba. "Functional analysis of two genes coding for distinct cation diffusion facilitators of the ectomycorrhizal Zn-accumulating fungus Russula atropurpurea." BioMetals 29, no. 2 (February 23, 2016): 349–63. http://dx.doi.org/10.1007/s10534-016-9920-x.

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8

Martin, Julia E., and David P. Giedroc. "Functional Determinants of Metal Ion Transport and Selectivity in Paralogous Cation Diffusion Facilitator Transporters CzcD and MntE in Streptococcus pneumoniae." Journal of Bacteriology 198, no. 7 (January 19, 2016): 1066–76. http://dx.doi.org/10.1128/jb.00975-15.

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ABSTRACTCation diffusion facilitators (CDFs) are a large family of divalent metal transporters that collectively possess broad metal specificity and contribute to intracellular metal homeostasis and virulence in bacterial pathogens.Streptococcus pneumoniaeexpresses two homologous CDF efflux transporters, MntE and CzcD. Cells lackingmntEorczcDare sensitive to manganese (Mn) or zinc (Zn) toxicity, respectively, and specifically accumulate Mn or Zn, respectively, thus suggesting that MntE selectively transports Mn, while CzcD transports Zn. Here, we probe the origin of this metal specificity using a phenotypic growth analysis of pneumococcal variants. Structural homology toEscherichia coliYiiP predicts that both MntE and CzcD are dimeric and each protomer harbors four pairs of conserved metal-binding sites, termed the A site, the B site, and the C1/C2 binuclear site. We find that single amino acid mutations within both the transmembrane domain A site and the B site in both CDFs result in a cellular metal sensitivity similar to that of the corresponding null mutants. However, multiple mutations in the predicted cytoplasmic C1/C2 cluster of MntE have no impact on cellular Mn resistance, in contrast to the analogous substitutions in CzcD, which do have on impact on cellular Zn resistance. Deletion of the MntE-specific C-terminal tail, present only in Mn-specific bacterial CDFs, resulted in only a modest growth phenotype. Further analysis of MntE-CzcD functional chimeric transporters showed that Asn and Asp in theND-DD A-site motif of MntE and the most N-terminal His in theHD-HD site A of CzcD (the specified amino acids are underlined) play key roles in transporter metal selectivity.IMPORTANCECation diffusion facilitator (CDF) proteins are divalent metal ion transporters that are conserved in organisms ranging from bacteria to humans and that play important roles in cellular physiology, from metal homeostasis and resistance to type I diabetes in vertebrates. The respiratory pathogenStreptococcus pneumoniaeexpresses two metal CDF transporters, CzcD and MntE. How CDFs achieve metal selectivity is unclear. We show here that CzcD and MntE are true paralogs, as CzcD transports zinc, while MntE selectively transports manganese. Through the use of an extensive collection of pneumococcal variants, we show that a primary determinant for metal selectivity is the A site within the transmembrane domain. This extends our understanding of how CDFs discriminate among transition metals.

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9

Raimunda, Daniel C., Isidro Abreu, Paula Mihelj, and Manuel González-Guerrero. "When Two's Company: New Evidences on Dual Fe/Co Selectivity of Transport in the Co2+-Exporting Cation Diffusion Facilitators (CoF-eCDF) Family." Biophysical Journal 118, no. 3 (February 2020): 131a. http://dx.doi.org/10.1016/j.bpj.2019.11.848.

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10

Grünberg, Karen, Cathrin Wawer, Bradley M. Tebo, and Dirk Schüler. "A Large Gene Cluster Encoding Several Magnetosome Proteins Is Conserved in Different Species of Magnetotactic Bacteria." Applied and Environmental Microbiology 67, no. 10 (October 1, 2001): 4573–82. http://dx.doi.org/10.1128/aem.67.10.4573-4582.2001.

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ABSTRACT In magnetotactic bacteria, a number of specific proteins are associated with the magnetosome membrane (MM) and may have a crucial role in magnetite biomineralization. We have cloned and sequenced the genes of several of these polypeptides in the magnetotactic bacterium Magnetospirillum gryphiswaldense that could be assigned to two different genomic regions. Except for mamA, none of these genes have been previously reported to be related to magnetosome formation. Homologous genes were found in the genome sequences ofM. magnetotacticum and magnetic coccus strain MC-1. The MM proteins identified display homology to tetratricopeptide repeat proteins (MamA), cation diffusion facilitators (MamB), and HtrA-like serine proteases (MamE) or bear no similarity to known proteins (MamC and MamD). A major gene cluster containing several magnetosome genes (including mamA and mamB) was found to be conserved in all three of the strains investigated. ThemamAB cluster also contains additional genes that have no known homologs in any nonmagnetic organism, suggesting a specific role in magnetosome formation.

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11

Satarug, Soisungwan, Scott H. Garrett, Seema Somji, Mary Ann Sens, and Donald A. Sens. "Aberrant Expression of ZIP and ZnT Zinc Transporters in UROtsa Cells Transformed to Malignant Cells by Cadmium." Stresses 1, no. 2 (April 22, 2021): 78–89. http://dx.doi.org/10.3390/stresses1020007.

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Maintenance of zinc homeostasis is pivotal to the regulation of cell growth, differentiation, apoptosis, and defense mechanisms. In mammalian cells, control of cellular zinc homeostasis is through zinc uptake, zinc secretion, and zinc compartmentalization, mediated by metal transporters of the Zrt-/Irt-like protein (ZIP) family and the Cation Diffusion Facilitators (CDF) or ZnT family. We quantified transcript levels of ZIP and ZnT zinc transporters expressed by non-tumorigenic UROtsa cells and compared with those expressed by UROtsa clones that were experimentally transformed to cancer cells by prolonged exposure to cadmium (Cd). Although expression of the ZIP8 gene in parent UROtsa cells was lower than ZIP14 (0.1 vs. 83 transcripts per 1000 β-actin transcripts), an increased expression of ZIP8 concurrent with a reduction in expression of one or two zinc influx transporters, namely ZIP1, ZIP2, and ZIP3, were seen in six out of seven transformed UROtsa clones. Aberrant expression of the Golgi zinc transporters ZIP7, ZnT5, ZnT6, and ZnT7 were also observed. One transformed clone showed distinctively increased expression of ZIP6, ZIP10, ZIP14, and ZnT1, with a diminished ZIP8 expression. These data suggest intracellular zinc dysregulation and aberrant zinc homeostasis both in the cytosol and in the Golgi in the transformed UROtsa clones. These results provide evidence for zinc dysregulation in transformed UROtsa cells that may contribute in part to their malignancy and/or muscle invasiveness.

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12

Zhong, Hua, Bao Ping Sun, and Fang Ying Zhao. "A Preliminary Bioinformatics Analysis of Cation Diffusion Facilitator (CDF) Proteins in Different Plants." Advanced Materials Research 282-283 (July 2011): 453–56. http://dx.doi.org/10.4028/www.scientific.net/amr.282-283.453.

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The amino acid sequence of Cation Diffusion Facilitator from Populus trichocarpa, Thlaspi goesingense, Arabidopsis lyrata subsp. Lyrata, Brassica juncea and Medicago sativa, registered in GenBank, were analyzed and researched by the bioinformatic tools in the several aspects, including hydrophobicity / hydrophilicity properties, post-translational modification, secondary structures prediction and transmembrane domain. The results showed that Cation Diffusion Facilitator is a hydrophobic and transmembrane protein, which exists in endoplasmic reticulum and other secretory pathway. The main motifs of predicted secondary structure of Cation Diffusion Facilitator are alpha helix and random coil.

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13

Kolaj-Robin, Olga, David Russell, Kevin A. Hayes, J. Tony Pembroke, and Tewfik Soulimane. "Cation Diffusion Facilitator family: Structure and function." FEBS Letters 589, no. 12 (April 17, 2015): 1283–95. http://dx.doi.org/10.1016/j.febslet.2015.04.007.

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14

Grover, Amit, and Rakesh Sharma. "Identification and Characterization of a Major Zn(II) Resistance Determinant of Mycobacterium smegmatis." Journal of Bacteriology 188, no. 19 (October 1, 2006): 7026–32. http://dx.doi.org/10.1128/jb.00643-06.

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ABSTRACT A zinc ion-sensitive mutant of Mycobacterium smegmatis was isolated. The transposon insertion was located in zitA (MSMEG0750), a gene coding for a cation diffusion facilitator family protein. Zinc ions specifically induced expression of zitA. In silico analysis revealed that environmental and opportunistic pathogenic species contain higher numbers of cation diffusion facilitator genes than do obligate pathogens.

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15

Jirakulaporn, Tanawat, and Anthony J. Muslin. "Cation Diffusion Facilitator Proteins Modulate Raf-1 Activity." Journal of Biological Chemistry 279, no. 26 (April 19, 2004): 27807–15. http://dx.doi.org/10.1074/jbc.m401210200.

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16

Munkelt, Doreen, Gregor Grass, and Dietrich H. Nies. "The Chromosomally Encoded Cation Diffusion Facilitator Proteins DmeF and FieF from Wautersia metallidurans CH34 Are Transporters of Broad Metal Specificity." Journal of Bacteriology 186, no. 23 (December 1, 2004): 8036–43. http://dx.doi.org/10.1128/jb.186.23.8036-8043.2004.

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ABSTRACT Genomic sequencing of the β-proteobacterium Wautersia (previously Ralstonia) metallidurans CH34 revealed the presence of three genes encoding proteins of the cation diffusion facilitator (CDF) family. One, CzcD, was previously found to be part of the high-level metal resistance system Czc that mediates the efflux of Co(II), Zn(II), and Cd(II) ions catalyzed by the CzcCBA cation-proton antiporter. The second CDF protein, FieF, is probably mainly a ferrous iron detoxifying protein but also mediated some resistance against other divalent metal cations such as Zn(II), Co(II), Cd(II), and Ni(II) in W. metallidurans or Escherichia coli. The third CDF protein, DmeF, showed the same substrate spectrum as FieF, but with different preferences. DmeF plays the central role in cobalt homeostasis in W. metallidurans, and a disruption of dmeF rendered the high-level metal cation resistance systems Czc and Cnr ineffective against Co(II). This is evidence for the periplasmic detoxification of substrates by RND transporters of the heavy metal efflux family subgroup.

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17

Barber-Zucker, Shiran, Jenny Hall, Afonso Froes, Sofiya Kolusheva, Fraser MacMillan, and Raz Zarivach. "The cation diffusion facilitator protein MamM's cytoplasmic domain exhibits metal-type dependent binding modes and discriminates against Mn2+." Journal of Biological Chemistry 295, no. 49 (September 23, 2020): 16614–29. http://dx.doi.org/10.1074/jbc.ra120.014145.

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Cation diffusion facilitator (CDF) proteins are a conserved family of divalent transition metal cation transporters. CDF proteins are usually composed of two domains: the transmembrane domain, in which the metal cations are transported through, and a regulatory cytoplasmic C-terminal domain (CTD). Each CDF protein transports either one specific metal or multiple metals from the cytoplasm, and it is not known whether the CTD takes an active regulatory role in metal recognition and discrimination during cation transport. Here, the model CDF protein MamM, an iron transporter from magnetotactic bacteria, was used to probe the role of the CTD in metal recognition and selectivity. Using a combination of biophysical and structural approaches, the binding of different metals to MamM CTD was characterized. Results reveal that different metals bind distinctively to MamM CTD in terms of their binding sites, thermodynamics, and binding-dependent conformations, both in crystal form and in solution, which suggests a varying level of functional discrimination between CDF domains. Furthermore, these results provide the first direct evidence that CDF CTDs play a role in metal selectivity. We demonstrate that MamM's CTD can discriminate against Mn2+, supporting its postulated role in preventing magnetite formation poisoning in magnetotactic bacteria via Mn2+ incorporation.

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18

Anton, Andreas, Cornelia Große, Jana Reißmann, Thomas Pribyl, and Dietrich H. Nies. "CzcD Is a Heavy Metal Ion Transporter Involved in Regulation of Heavy Metal Resistance in Ralstonia sp. Strain CH34." Journal of Bacteriology 181, no. 22 (November 15, 1999): 6876–81. http://dx.doi.org/10.1128/jb.181.22.6876-6881.1999.

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ABSTRACT The Czc system of Ralstonia sp. strain CH34 mediates resistance to cobalt, zinc, and cadmium through ion efflux catalyzed by the CzcCB2A cation-proton antiporter. The CzcD protein is involved in the regulation of the Czc system. It is a membrane-bound protein with at least four transmembrane α-helices and is a member of a subfamily of the cation diffusion facilitator (CDF) protein family, which occurs in all three domains of life. The deletion ofczcD in a Ralstonia sp. led to partially constitutive expression of the Czc system due to an increased transcription of the structural czcCBA genes, both in the absence and presence of inducers. The czcD deletion could be fully complemented in trans by CzcD and two other CDF proteins from Saccharomyces cerevisiae, ZRC1p and COT1p. All three proteins mediated a small but significant resistance to cobalt, zinc, and cadmium in Ralstonia, and this resistance was based on a reduced accumulation of the cations. Thus, CzcD appeared to repress the Czc system by an export of the inducing cations.

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19

Barber-Zucker, Shiran, Arie Moran, and Raz Zarivach. "Metal transport mechanism of the cation diffusion facilitator (CDF) protein family – a structural perspective on human CDF (ZnT)-related diseases." RSC Chemical Biology 2, no. 2 (2021): 486–98. http://dx.doi.org/10.1039/d0cb00181c.

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20

Shusterman, Eden, Ofer Beharier, Levy Shiri, Raz Zarivach, Yoram Etzion, Craig R. Campbell, Il-Ha Lee, et al. "ZnT-1 extrudes zinc from mammalian cells functioning as a Zn2+/H+exchanger." Metallomics 6, no. 9 (2014): 1656–63. http://dx.doi.org/10.1039/c4mt00108g.

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21

Ibuot, Aniefon, Andrew P. Dean, and Jon K. Pittman. "Multi-genomic analysis of the cation diffusion facilitator transporters from algae." Metallomics 12, no. 4 (2020): 617–30. http://dx.doi.org/10.1039/d0mt00009d.

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Cation diffusion facilitator metal transporters are widespread throughout algae and include a novel algal-specific clade. Functional analysis of Chlamydomonas reinhardtii isoforms partly validated phylogenetic prediction of substrate specificity.

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22

Zogzas, Charles E., and Somshuvra Mukhopadhyay. "Putative metal binding site in the transmembrane domain of the manganese transporter SLC30A10 is different from that of related zinc transporters." Metallomics 10, no. 8 (2018): 1053–64. http://dx.doi.org/10.1039/c8mt00115d.

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23

Davis, Diana E., Hyun Cheol Roh, Krupa Deshmukh, Janelle J. Bruinsma, Daniel L. Schneider, James Guthrie, J. David Robertson, and Kerry Kornfeld. "The Cation Diffusion Facilitator Genecdf-2Mediates Zinc Metabolism inCaenorhabditis elegans." Genetics 182, no. 4 (May 17, 2009): 1015–33. http://dx.doi.org/10.1534/genetics.109.103614.

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24

Lopez, Maria L., Akiko Koide, Lorena Novoa, Jose M. Arguello, Shohei Koide, and David L. Stokes. "Zinc-Induced Conformational Changes in the Cation Diffusion Facilitator YiiP." Biophysical Journal 118, no. 3 (February 2020): 440a—441a. http://dx.doi.org/10.1016/j.bpj.2019.11.2468.

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25

Peiter, E., B. Montanini, A. Gobert, P. Pedas, S. Husted, F. J. M. Maathuis, D. Blaudez, M. Chalot, and D. Sanders. "A secretory pathway-localized cation diffusion facilitator confers plant manganese tolerance." Proceedings of the National Academy of Sciences 104, no. 20 (May 9, 2007): 8532–37. http://dx.doi.org/10.1073/pnas.0609507104.

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26

Haney, Christopher J., Gregor Grass, Sylvia Franke, and Christopher Rensing. "New developments in the understanding of the cation diffusion facilitator family." Journal of Industrial Microbiology & Biotechnology 32, no. 6 (May 12, 2005): 215–26. http://dx.doi.org/10.1007/s10295-005-0224-3.

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27

Zhang, Wei, Xiliang Liao, Yanmei Cui, Weiyu Ma, Xinnan Zhang, Hongyang Du, Yujie Ma, et al. "A cation diffusion facilitator, GmCDF1, negatively regulates salt tolerance in soybean." PLOS Genetics 15, no. 1 (January 7, 2019): e1007798. http://dx.doi.org/10.1371/journal.pgen.1007798.

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28

Bruinsma, Janelle J., Tanawat Jirakulaporn, Anthony J. Muslin, and Kerry Kornfeld. "Zinc Ions and Cation Diffusion Facilitator Proteins Regulate Ras-Mediated Signaling." Developmental Cell 2, no. 5 (May 2002): 567–78. http://dx.doi.org/10.1016/s1534-5807(02)00151-x.

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29

Cubillas, Ciro, Pablo Vinuesa, Maria Luisa Tabche, and Alejandro García-de los Santos. "Phylogenomic analysis of Cation Diffusion Facilitator proteins uncovers Ni2+/Co2+ transporters." Metallomics 5, no. 12 (2013): 1634. http://dx.doi.org/10.1039/c3mt00204g.

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30

Lopez, Maria L., Akiko Koide, Lorena Novoa Aponte, Shujie Fan, Oliver Beckstein, Jose M. Arguello, Shohei Koide, and David L. Stokes. "Role of Individual Zinc Binding Sites in the Cation Diffusion Facilitator YIIP." Biophysical Journal 120, no. 3 (February 2021): 104a. http://dx.doi.org/10.1016/j.bpj.2020.11.845.

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31

Hussein, Adel K., Maria L. Lopez-Redondo, Xihui Zhang, and David L. Stokes. "Characterization of individual zinc binding sites in the cation diffusion facilitator YiiP." Biophysical Journal 121, no. 3 (February 2022): 252a. http://dx.doi.org/10.1016/j.bpj.2021.11.1509.

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32

Russell, David, Olga Kolaj-Robin, and Tewfik Soulimane. "Maricaulis maris cation diffusion facilitator: Achieving homogeneity through a mixed-micelle approach." Protein Expression and Purification 85, no. 2 (October 2012): 173–80. http://dx.doi.org/10.1016/j.pep.2012.07.011.

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33

Grass, Gregor, Bin Fan, Barry P. Rosen, Sylvia Franke, Dietrich H. Nies, and Christopher Rensing. "ZitB (YbgR), a Member of the Cation Diffusion Facilitator Family, Is an Additional Zinc Transporter inEscherichia coli." Journal of Bacteriology 183, no. 15 (August 1, 2001): 4664–67. http://dx.doi.org/10.1128/jb.183.15.4664-4667.2001.

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ABSTRACT The Escherichia coli zitB gene encodes a Zn(II) transporter belonging to the cation diffusion facilitator family. ZitB is specifically induced by zinc. ZitB expression on a plasmid renderedzntA-disrupted E. coli cells more resistant to zinc, and the cells exhibited reduced accumulation of 65Zn, suggesting ZitB-mediated efflux of zinc.

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34

Guffanti, Arthur A., Yi Wei, Sacha V. Rood, and Terry A. Krulwich. "An antiport mechanism for a member of the cation diffusion facilitator family: divalent cations efflux in exchange for K+ and H+." Molecular Microbiology 45, no. 1 (July 2002): 145–53. http://dx.doi.org/10.1046/j.1365-2958.2002.02998.x.

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35

Lopez-Redondo, Maria Luisa, Nicolas Coudray, Zhening Zhang, John Alexopoulos, and David L. Stokes. "Structural basis for the alternating access mechanism of the cation diffusion facilitator YiiP." Proceedings of the National Academy of Sciences 115, no. 12 (March 5, 2018): 3042–47. http://dx.doi.org/10.1073/pnas.1715051115.

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YiiP is a dimeric antiporter from the cation diffusion facilitator family that uses the proton motive force to transport Zn2+ across bacterial membranes. Previous work defined the atomic structure of an outward-facing conformation, the location of several Zn2+ binding sites, and hydrophobic residues that appear to control access to the transport sites from the cytoplasm. A low-resolution cryo-EM structure revealed changes within the membrane domain that were associated with the alternating access mechanism for transport. In the current work, the resolution of this cryo-EM structure has been extended to 4.1 Å. Comparison with the X-ray structure defines the differences between inward-facing and outward-facing conformations at an atomic level. These differences include rocking and twisting of a four-helix bundle that harbors the Zn2+ transport site and controls its accessibility within each monomer. As previously noted, membrane domains are closely associated in the dimeric structure from cryo-EM but dramatically splayed apart in the X-ray structure. Cysteine crosslinking was used to constrain these membrane domains and to show that this large-scale splaying was not necessary for transport activity. Furthermore, dimer stability was not compromised by mutagenesis of elements in the cytoplasmic domain, suggesting that the extensive interface between membrane domains is a strong determinant of dimerization. As with other secondary transporters, this interface could provide a stable scaffold for movements of the four-helix bundle that confers alternating access of these ions to opposite sides of the membrane.

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36

Delhaize, Emmanuel, Tatsuhiko Kataoka, Diane M. Hebb, Rosemary G. White, and Peter R. Ryan. "Genes Encoding Proteins of the Cation Diffusion Facilitator Family That Confer Manganese Tolerance." Plant Cell 15, no. 5 (May 2003): 1131–42. http://dx.doi.org/10.1105/tpc.009134.

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37

Higuchi, Takashi, Motoyuki Hattori, Yoshiki Tanaka, Ryuichiro Ishitani, and Osamu Nureki. "Crystal structure of the cytosolic domain of the cation diffusion facilitator family protein." Proteins: Structure, Function, and Bioinformatics 76, no. 3 (August 15, 2009): 768–71. http://dx.doi.org/10.1002/prot.22444.

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38

Borkovska, L. V., R. Beyer, M. Hoffmann, A. Holzhey, N. Korsunska, Yu G. Sadofyev, and Joerg Weber. "Role of Cation Vacancy-Related Defects in Self-Assembling of CdSe Quantum Dots." Defect and Diffusion Forum 230-232 (November 2004): 55–66. http://dx.doi.org/10.4028/www.scientific.net/ddf.230-232.55.

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In this chapter we present the results of the photoluminescent and optical investigations of the influence of cation vacancy-related defects on CdSe/ZnSe quantum dot organization. Selfassembling growth was achieved under molecular beam epitaxy with subsequent annealing step. Number of cation vacancies was controlled by the intensity of the emission band connected with complex that includes cation vacancy and shallow donor. For the first time it is shown that increase of number of cation vacancy related defects results in the reduction of potential fluctuations in the QD layer. In this case a relatively uniform dense array of QDs with shallow localization potential is organized. It is proposed that generation of cation vacancies during the growth suppresses both Cd segregation and Cd surface diffusion as well as facilitates Cd/Zn interdiffusion. Interdiffusion process is proved by the changes in the photoluminescence and optical reflection spectra of ZnSe layers. It is showned that Cd/Zn interdiffusion can play an important role in CdSe/ZnSe intermixing during the QD formation at least under such growth conditions which can stimulate generation of cation vacancies.

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Chen, Zonghui, Yumi Fujii, Naoki Yamaji, Sakine Masuda, Yuma Takemoto, Takehiro Kamiya, Yusufujiang Yusuyin, et al. "Mn tolerance in rice is mediated by MTP8.1, a member of the cation diffusion facilitator family." Journal of Experimental Botany 64, no. 14 (August 20, 2013): 4375–87. http://dx.doi.org/10.1093/jxb/ert243.

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Fang, Yue, Reiko Sugiura, Yan Ma, Tomoko Yada-Matsushima, Hirotatsu Umeno, and Takayoshi Kuno. "Cation Diffusion Facilitator Cis4 Is Implicated in Golgi Membrane Trafficking via Regulating Zinc Homeostasis in Fission Yeast." Molecular Biology of the Cell 19, no. 4 (April 2008): 1295–303. http://dx.doi.org/10.1091/mbc.e07-08-0805.

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We screened for mutations that confer sensitivities to the calcineurin inhibitor FK506 and to a high concentration of MgCl2 and isolated the cis4-1 mutant, an allele of the gene encoding a cation diffusion facilitator (CDF) protein that is structurally related to zinc transporters. Consistently, the addition of extracellular Zn2+ suppressed the phenotypes of the cis4 mutant cells. The cis4 mutants and the mutant cells of another CDF-encoding gene SPBC16E9.14c (we named zrg17+) shared common and nonadditive zinc-suppressible phenotypes, and Cis4 and Zrg17 physically interacted. Cis4 localized at the cis-Golgi, suggesting that Cis4 is responsible for Zn2+ uptake to the cis-Golgi. The cis4 mutant cells showed phenotypes such as weak cell wall and decreased acid phosphatase secretion that are thought to be resulting from impaired membrane trafficking. In addition, the cis4 deletion cells showed synthetic growth defects with all the four membrane-trafficking mutants tested, namely ypt3-i5, ryh1-i6, gdi1-i11, and apm1-1. Interestingly, the addition of extracellular Zn2+ significantly suppressed the phenotypes of the ypt3-i5 and apm1-1 mutant cells. These results suggest that Cis4 forms a heteromeric functional complex with Zrg17 and that Cis4 is implicated in Golgi membrane trafficking through the regulation of zinc homeostasis in fission yeast.

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González-Guerrero, Manuel, Concepción Azcón-Aguilar, Michelle Mooney, Ascensión Valderas, Colin W. MacDiarmid, David J. Eide, and Nuria Ferrol. "Characterization of a Glomus intraradices gene encoding a putative Zn transporter of the cation diffusion facilitator family." Fungal Genetics and Biology 42, no. 2 (February 2005): 130–40. http://dx.doi.org/10.1016/j.fgb.2004.10.007.

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Li, Liangtao, and Jerry Kaplan. "The Yeast GeneMSC2, a Member of the Cation Diffusion Facilitator Family, Affects the Cellular Distribution of Zinc." Journal of Biological Chemistry 276, no. 7 (October 31, 2000): 5036–43. http://dx.doi.org/10.1074/jbc.m008969200.

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Peterson, R. H., and D. J. Martin-Robichaud. "Permeability of the Isolated Atlantic Salmon (Salmo salar) Chorion to Ions as Estimated by Diffusion Potentials." Canadian Journal of Fisheries and Aquatic Sciences 44, no. 9 (September 1, 1987): 1635–39. http://dx.doi.org/10.1139/f87-198.

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The properties of the teleost chorion and perivitelline fluid may allow the embryo to develop in an ionic medium which differs from ambient. A knowledge of these properties facilitates assessment of the potential impact of environmental perturbations (e.g. low-pH episodes) on the developing embryo. Diffusion potentials are created when differing concentrations of a salt solution are imposed upon the opposite sides of isolated Atlantic salmon (Salmo salar) chorions. These diffusion potentials are related to the mobilities of the cations and anions. The magnitude of the diffusion potentials were measured with NaCl, CaC2, H2SO4, and HCl solutions. The results indicate that both anions and cations permeate the chorion. Chloride appears to have greater mobility through the chorion than does sodium, although the difference in mobility of such ion pairs moving through the chorion is not as great as the difference in their mobilities in aqueous solution. Diffusion potentials obtained with CaCl2 solutions, on the other hand, indicate reduced calcium mobility through the chorion relative to chloride. The decreased mobility of Ca2+ is probably due to adsorption to fixed negative charges on the chorion. The properties of the perivitelline potential of the intact egg could be simulated qualitatively by placing a solution of negatively charged colloid (hen's egg albumin) inside the isolated chorion.

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Hattori, Motoyuki, Yoshiki Tanaka, Ryuichiro Ishitani, and Osamu Nureki. "Crystallization and preliminary X-ray diffraction analysis of the cytosolic domain of a cation diffusion facilitator family protein." Acta Crystallographica Section F Structural Biology and Crystallization Communications 63, no. 9 (August 25, 2007): 771–73. http://dx.doi.org/10.1107/s1744309107038948.

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Goswami, Devrishi, Jagdeep Kaur, Sachin Surade, Ernst Grell, and Hartmut Michel. "Heterologous production and functional and thermodynamic characterization of cation diffusion facilitator (CDF) transporters of mesophilic and hyperthermophilic origin." Biological Chemistry 393, no. 7 (July 1, 2012): 617–29. http://dx.doi.org/10.1515/hsz-2012-0101.

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Abstract The members of the cation diffusion facilitator (CDF) family transport heavy metal ions and play an important function in zinc ion homeostasis of the cell. A recent structure of an Escherichia coli CDF transporter protein YiiP has revealed its dimeric nature and autoregulatory zinc transport mechanism. Here, we report the cloning and heterologous production of four different CDF transporters, two each from the pathogenic mesophilic bacterium Salmonella typhimurium and from the hyperthermophilic bacterium Aquifex aeolicus, in E. coli host cells. STM0758 of S. typhimurium was able to restore resistance to zinc ions when tested by complementation assays in the zinc-sensitive GG48 strain. Furthermore, copurification of bicistronically produced STM0758 and cross-linking experiments with the purified protein have revealed its possible oligomeric nature. The interaction between heavy metal ions and Aq_2073 of A. aeolicus was investigated by titration calorimetry. The entropy-driven, high-affinity binding of two Cd2+ and two Zn2+ per protein monomer with Kd values of around 100 nm and 1 μm, respectively, was observed. In addition, at least one more Zn2+ can be bound per monomer with low affinity. This low-affinity site is likely to possess a functional role contributing to Zn2+ transport across membranes.

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Montanini, Barbara, Damien Blaudez, Sylvain Jeandroz, Dale Sanders, and Michel Chalot. "Phylogenetic and functional analysis of the Cation Diffusion Facilitator (CDF) family: improved signature and prediction of substrate specificity." BMC Genomics 8, no. 1 (2007): 107. http://dx.doi.org/10.1186/1471-2164-8-107.

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Tsunemitsu, Yuta, Mayuko Genga, Tomoyuki Okada, Naoki Yamaji, Jian Feng Ma, Akira Miyazaki, Shin-ichiro Kato, Kozo Iwasaki, and Daisei Ueno. "A member of cation diffusion facilitator family, MTP11, is required for manganese tolerance and high fertility in rice." Planta 248, no. 1 (April 26, 2018): 231–41. http://dx.doi.org/10.1007/s00425-018-2890-1.

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Jiang, Hai-Bo, Wen-Jing Lou, Han-Ying Du, Neil M. Price, and Bao-Sheng Qiu. "Sll1263, a Unique Cation Diffusion Facilitator Protein that Promotes Iron Uptake in the Cyanobacterium Synechocystis sp. Strain PCC 6803." Plant and Cell Physiology 53, no. 8 (June 7, 2012): 1404–17. http://dx.doi.org/10.1093/pcp/pcs086.

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Takeno, Seiki, Mio Nakamura, Rie Fukai, Junko Ohnishi, and Masato Ikeda. "The Cgl1281-encoding putative transporter of the cation diffusion facilitator family is responsible for alkali-tolerance in Corynebacterium glutamicum." Archives of Microbiology 190, no. 5 (July 1, 2008): 531–38. http://dx.doi.org/10.1007/s00203-008-0401-7.

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Yu, Xinti, Zechuan Yu, Heng Zhao, Ian D. Gates, and Jinguang Hu. "Photothermal catalytic H2 production over hierarchical porous CaTiO3 with plasmonic gold nanoparticles." Chemical Synthesis 3, no. 1 (2023): 3. http://dx.doi.org/10.20517/cs.2022.30.

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The synergistic promotion by photocatalysis and thermocatalysis is a promising approach for sustainable hydrogen (H2) production. Herein, we rationally design a perovskite-based catalyst with three-dimensionally ordered macroporous structure (3DOM CaTiO3-Au) for photothermal catalytic H2 production from different substrates. The hierarchical 3DOM structure facilitates light harvesting and mass diffusion of the substrates, while the gold nanoparticles (Au NPs) promote charge separation. The photogenerated and hot electrons are oriented accumulated on the surface of Au NPs. The non-metallic gold species [Au(I)] show more activity for H2 evolution. As a result, 3DOM CaTiO3-Au exhibits excellent activity for H2 production from glycerol and other substrates with hydroxyl groups. The present work demonstrates a feasible approach to improve sustainable H2 production by rationally designing and fabricating efficient photothermal catalysts.

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