Document Detail


Cyanobacterial metallochaperone inhibits deleterious side reactions of copper.
MedLine Citation:
PMID:  22198771     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Copper metallochaperones supply copper to cupro-proteins through copper-mediated protein-protein-interactions and it has been hypothesized that metallochaperones thereby inhibit copper from causing damage en route. Evidence is presented in support of this latter role for cyanobacterial metallochaperone, Atx1. In cyanobacteria Atx1 contributes towards the supply of copper to plastocyanin inside thylakoids but it is shown here that in copper-replete medium, copper can reach plastocyanin without Atx1. Unlike metallochaperone-independent copper-supply to superoxide dismutase in eukaryotes, glutathione is not essential for Atx1-independent supply to plastocyanin: Double mutants missing atx1 and gshB (encoding glutathione synthetase) accumulate the same number of atoms of copper per cell in the plastocyanin pool as wild type. Critically, Δatx1ΔgshB are hypersensitive to elevated copper relative to wild type cells and also relative to ΔgshB single mutants with evidence that hypersensitivity arises due to the mislocation of copper to sites for other metals including iron and zinc. The zinc site on the amino-terminal domain (ZiaA(N)) of the P(1)-type zinc-transporting ATPase is especially similar to the copper site of the Atx1 target PacS(N), and ZiaA(N) will bind Cu(I) more tightly than zinc. An NMR model of a substituted-ZiaA(N)-Cu(I)-Atx1 heterodimer has been generated making it possible to visualize a juxtaposition of residues surrounding the ZiaA(N) zinc site, including Asp(18), which normally repulse Atx1. Equivalent repulsion between bacterial copper metallochaperones and the amino-terminal regions of P(1)-type ATPases for metals other than Cu(I) is conserved, again consistent with a role for copper metallochaperones to withhold copper from binding sites for other metals.
Authors:
Steve Tottey; Carl J Patterson; Lucia Banci; Ivano Bertini; Isabella C Felli; Anna Pavelkova; Samantha J Dainty; Rafael Pernil; Kevin J Waldron; Andrew W Foster; Nigel J Robinson
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2011-12-22
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  109     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2012 Jan 
Date Detail:
Created Date:  2012-01-05     Completed Date:  2012-03-06     Revised Date:  2014-11-05    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  95-100     Citation Subset:  IM    
Data Bank Information
Bank Name/Acc. No.:
PDB/2LDI
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / metabolism
Bacterial Proteins / metabolism
Copper / pharmacology,  toxicity*
Culture Media / pharmacology
Glutathione / metabolism
Homeostasis / drug effects
Metallochaperones / metabolism*
Models, Molecular
Mutation / genetics
Plastocyanin / metabolism
Protein Binding / drug effects
Synechocystis / drug effects*,  metabolism*
Zinc / metabolism
Grant Support
ID/Acronym/Agency:
BB/E001688/1//Biotechnology and Biological Sciences Research Council; BB/H006052/2//Biotechnology and Biological Sciences Research Council; BB/H011110/1//Biotechnology and Biological Sciences Research Council; BBS/B/02576//Biotechnology and Biological Sciences Research Council
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Culture Media; 0/Metallochaperones; 789U1901C5/Copper; 9014-09-9/Plastocyanin; EC 3.6.1.-/Adenosine Triphosphatases; GAN16C9B8O/Glutathione; J41CSQ7QDS/Zinc
Comments/Corrections

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