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PMID:11739376

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Citation

Tottey, S, Rondet, SA, Borrelly, GP, Robinson, PJ, Rich, PR and Robinson, NJ (2002) A copper metallochaperone for photosynthesis and respiration reveals metal-specific targets, interaction with an importer, and alternative sites for copper acquisition. J. Biol. Chem. 277:5490-7

Abstract

A bacterial two-hybrid assay revealed interaction between a protein now designated bacterial Atx1 and amino-terminal domains of copper-transporting ATPases CtaA (cellular import) and PacS (thylakoid import) but not the related zinc (ZiaA) or cobalt (CoaT) transporters from the same organism (Synechocystis PCC 6803). The specificity of metallochaperone interactions coincides with metal specificity. After reconstitution in a N(2) atmosphere, bacterial Atx1 bound 1 mol of copper mol(-1), and apoPacS(N) acquired copper from copper-Atx1. Copper was displaced from Atx1 by p-(hydroxymercuri)phenylsulfonate, indicative of thiol ligands, and two cysteine residues were obligatory for two-hybrid interaction with PacS(N). This organism contains compartments (thylakoids) where the copper proteins plastocyanin and cytochrome oxidase reside. In copper super-supplemented mutants, photooxidation of cytochrome c(6) was greater in Deltaatx1DeltactaA than in DeltactaA, showing that Atx1 contributes to efficient switching from iron in cytochrome c(6) to copper in plastocyanin for photosynthetic electron transport. Cytochrome oxidase activity was also less in membranes purified from low [copper]-grown Deltaatx1 or DeltapacS, compared with wild-type, but the double mutant Deltaatx1DeltapacS was non-additive, consistent with Atx1 acting via PacS. Conversely, activity in Deltaatx1DeltactaA was less than in either respective single mutant, revealing that Atx1 can function without the major copper importer and consistent with a role in recycling endogenous copper.

Links

PubMed Online version:10.1074/jbc.M105857200

Keywords

ATP-Binding Cassette Transporters; Adenosine Triphosphatases/metabolism; Amino Acid Motifs; Amino Acid Sequence; Bacterial Proteins; Binding Sites; Blotting, Southern; Carrier Proteins/chemistry; Carrier Proteins/genetics; Carrier Proteins/metabolism; Cation Transport Proteins/metabolism; Cell Membrane/metabolism; Cloning, Molecular; Copper/chemistry; Cyanobacteria/metabolism; Cysteine/chemistry; Cytochrome b Group/chemistry; Cytochrome b Group/genetics; Cytochromes/metabolism; Cytochromes f; DNA/metabolism; Electron Transport Complex IV/metabolism; Fungal Proteins/chemistry; Fungal Proteins/genetics; Kinetics; Ligands; Membrane Proteins/chemistry; Membrane Proteins/genetics; Models, Molecular; Molecular Sequence Data; Mutation; Oxygen/metabolism; Phenotype; Photosynthesis; Plastocyanin/metabolism; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins/metabolism; Saccharomyces cerevisiae Proteins; Sequence Homology, Amino Acid; Thylakoids/chemistry; Time Factors; Two-Hybrid System Techniques; beta-Galactosidase/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

SYNY3:P73213

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P73241

F

Seeded From UniProt

complete

SYNY3:P73213

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P74512

F

Seeded From UniProt

complete

SYNY3:ATCS

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P73213

F

Seeded From UniProt

complete

SYNY3:ATCS

enables

GO:0005507: copper ion binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

SYNY3:ATCS

involved_in

GO:0015677: copper ion import

ECO:0000304: author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

SYNY3:P74512

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P73213

F

Seeded From UniProt

complete


See also

References

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