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Literature DB >> 16412426

Interactions of the Escherichia coli hydrogenase biosynthetic proteins: HybG complex formation.

Gareth Butland¹, Jie Wei Zhang, Wenhong Yang, Anthony Sheung, Peter Wong, Jack F Greenblatt, Andrew Emili, Deborah B Zamble.

Abstract

Assembly of the active site of the [NiFe]-hydrogenase enzymes involves a multi-step pathway and the coordinated activity of many accessory proteins. To analyze complex formation between these factors in Escherichia coli, they were genomically tagged and native multi-protein complexes were isolated. This method validated multiple interactions reported in separate studies from several organisms and defined a new complex containing the putative chaperone HybG and the large subunit of hydrogenase 1 or 2. The complex also includes HypE and HypD, which interact with each other before joining the larger complex.

Entities: Gene Species

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Year: 2005 PMID： 16412426 DOI： 10.1016/j.febslet.2005.12.063

Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124

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Cited

9 in total

1. Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase.

Authors: Kim C Chan Chung; Deborah B Zamble
Journal: J Biol Chem Date: 2011-10-20 Impact factor: 5.157

2. Coordination of Synthesis and Assembly of a Modular Membrane-Associated [NiFe]-Hydrogenase Is Determined by Cleavage of the C-Terminal Peptide.

Authors: Claudia Thomas; Enrico Muhr; R Gary Sawers
Journal: J Bacteriol Date: 2015-07-13 Impact factor: 3.490

3. Proteolytic cleavage orchestrates cofactor insertion and protein assembly in [NiFe]-hydrogenase biosynthesis.

Authors: Moritz Senger; Sven T Stripp; Basem Soboh
Journal: J Biol Chem Date: 2017-05-24 Impact factor: 5.157

4. Modularity analysis based on predicted protein-protein interactions provides new insights into pathogenicity and cellular process of Escherichia coli O157:H7.

Authors: Xia Wang; Junjie Yue; Xianwen Ren; Yuelan Wang; Mingfeng Tan; Beiping Li; Long Liang
Journal: Theor Biol Med Model Date: 2011-12-22 Impact factor: 2.432

Interactions of the Escherichia coli hydrogenase biosynthetic proteins: HybG complex formation.

1. Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase.

2. Coordination of Synthesis and Assembly of a Modular Membrane-Associated [NiFe]-Hydrogenase Is Determined by Cleavage of the C-Terminal Peptide.

3. Proteolytic cleavage orchestrates cofactor insertion and protein assembly in [NiFe]-hydrogenase biosynthesis.

4. Modularity analysis based on predicted protein-protein interactions provides new insights into pathogenicity and cellular process of Escherichia coli O157:H7.

5. Efficient α, β-motif finder for identification of phenotype-related functional modules.

6. In-silico identification of phenotype-biased functional modules.

7. Interactome of Arabidopsis Thaliana.

8. SPICE: discovery of phenotype-determining component interplays.

9. Phyletic profiling with cliques of orthologs is enhanced by signatures of paralogy relationships.