Faculty Opinions recommendation of A secretory pathway-localized cation diffusion facilitator confers plant manganese tolerance.

Author(s):  
Nicolaus Von Wiren
2007 ◽  
Vol 104 (20) ◽  
pp. 8532-8537 ◽  
Author(s):  
E. Peiter ◽  
B. Montanini ◽  
A. Gobert ◽  
P. Pedas ◽  
S. Husted ◽  
...  

2011 ◽  
Vol 282-283 ◽  
pp. 453-456
Author(s):  
Hua Zhong ◽  
Bao Ping Sun ◽  
Fang Ying Zhao

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.


2003 ◽  
Vol 15 (5) ◽  
pp. 1131-1142 ◽  
Author(s):  
Emmanuel Delhaize ◽  
Tatsuhiko Kataoka ◽  
Diane M. Hebb ◽  
Rosemary G. White ◽  
Peter R. Ryan

Planta ◽  
2018 ◽  
Vol 248 (1) ◽  
pp. 231-241 ◽  
Author(s):  
Yuta Tsunemitsu ◽  
Mayuko Genga ◽  
Tomoyuki Okada ◽  
Naoki Yamaji ◽  
Jian Feng Ma ◽  
...  

2018 ◽  
Vol 115 (12) ◽  
pp. 3042-3047 ◽  
Author(s):  
Maria Luisa Lopez-Redondo ◽  
Nicolas Coudray ◽  
Zhening Zhang ◽  
John Alexopoulos ◽  
David L. Stokes

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.


2019 ◽  
Author(s):  
Aniefon Ibuot ◽  
Andrew P. Dean ◽  
Jon K. Pittman

AbstractMetal transport processes are relatively poorly understood in algae in comparison to higher plants and other eukaryotes. A screen of genomes from 33 taxonomically diverse algal species was conducted to identify members of the Cation Diffusion Facilitator (CDF) family of metal ion transporter. All algal genomes contained at least one CDF gene with four species having >10 CDF genes (median of 5 genes per genome), further confirming that this is a ubiquitous gene family. Phylogenetic analysis suggested a CDF gene organisation of five groups, which includes Zn-CDF, Fe/Zn-CDF and Mn-CDF groups, consistent with previous phylogenetic analyses, and two functionally undefined groups. One of these undefined groups was algal specific although excluded chlorophyte and rhodophyte sequences. The majority of sequences (22 out of 26 sequences) from this group had a putative ion binding site motif within transmembrane domain 2 and 5 that was distinct from other CDF proteins, such that alanine or serine replaced the conserved histidine residue. The phylogenetic grouping was supported by sequence cluster analysis. Yeast heterologous expression of CDF proteins from Chlamydomonas reinhardtii indicated Zn2+ and Co2+ transport function by CrMTP1, and Mn2+ transport function by CrMTP2, CrMTP3 and CrMTP4, which validated the phylogenetic prediction. However, the Mn-CDF protein CrMTP3 was also able to provide zinc and cobalt tolerance to the Zn- and Co-sensitive zrc1cot1 yeast strain. There is wide diversity of CDF transporters within the algae lineage, and some of these genes may be attractive targets for future applications of metal content engineering in plants or microorganisms.


2019 ◽  
Vol 202 (1) ◽  
Author(s):  
Matthew J. Johnsrude ◽  
Joshua E. Pitzer ◽  
Daniel W. Martin ◽  
R. Martin Roop

Mn nutrition is essential for the basic physiology and virulence of Brucella strains. The results of the study presented here demonstrate that the cation diffusion facilitator (CDF)-type metal exporter EmfA plays critical roles in maintaining Mn homeostasis and preventing Mn toxicity in Brucella and is an essential virulence determinant for these bacteria. EmfA and other cellular components involved in Mn homeostasis represent attractive targets for the development of improved vaccines and chemotherapeutic strategies for preventing and treating brucellosis in humans and animals.


2009 ◽  
Vol 76 (3) ◽  
pp. 768-771 ◽  
Author(s):  
Takashi Higuchi ◽  
Motoyuki Hattori ◽  
Yoshiki Tanaka ◽  
Ryuichiro Ishitani ◽  
Osamu Nureki

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