PMID:21498507
| Citation |
Lin, J and Wilson, MA (2011) Escherichia coli thioredoxin-like protein YbbN contains an atypical tetratricopeptide repeat motif and is a negative regulator of GroEL. J. Biol. Chem. 286:19459-69 |
|---|---|
| Abstract |
Many proteins contain a thioredoxin (Trx)-like domain fused with one or more partner domains that diversify protein function by the modular construction of new molecules. The Escherichia coli protein YbbN is a Trx-like protein that contains a C-terminal domain with low homology to tetratricopeptide repeat motifs. YbbN has been proposed to act as a chaperone or co-chaperone that aids in heat stress response and DNA synthesis. We report the crystal structure of YbbN, which is an elongated molecule with a mobile Trx domain and four atypical tetratricopeptide repeat motifs. The Trx domain lacks a canonical CXXC active site architecture and is not a functional oxidoreductase. A variety of proteins in E. coli interact with YbbN, including multiple ribosomal protein subunits and a strong interaction with GroEL. YbbN acts as a mild inhibitor of GroESL chaperonin function and ATPase activity, suggesting that it is a negative regulator of the GroESL system. Combined with previous observations that YbbN enhances the DnaK-DnaJ-GrpE chaperone system, we propose that YbbN coordinately regulates the activities of these two prokaryotic chaperones, thereby helping to direct client protein traffic initially to DnaK. Therefore, YbbN may play a role in integrating the activities of different chaperone pathways in E. coli and related bacteria. |
| Links |
PubMed PMC3103325 Online version:10.1074/jbc.M111.238741 |
| Keywords |
Amino Acid Motifs; Chaperonin 60/antagonists & inhibitors; Chaperonin 60/chemistry; Chaperonin 60/genetics; Chaperonin 60/metabolism; Crystallography, X-Ray; Enzyme Inhibitors/chemistry; Enzyme Inhibitors/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; HSP40 Heat-Shock Proteins/chemistry; HSP40 Heat-Shock Proteins/genetics; HSP40 Heat-Shock Proteins/metabolism; HSP70 Heat-Shock Proteins/chemistry; HSP70 Heat-Shock Proteins/genetics; HSP70 Heat-Shock Proteins/metabolism; Heat-Shock Proteins/chemistry; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Molecular Chaperones/chemistry; Molecular Chaperones/genetics; Molecular Chaperones/metabolism; Oxidoreductases Acting on Sulfur Group Donors/chemistry; Oxidoreductases Acting on Sulfur Group Donors/genetics; Oxidoreductases Acting on Sulfur Group Donors/metabolism; Protein Structure, Tertiary |
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