|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
22
|
|
pubmed:dateCreated |
2011-5-30
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
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.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chaperonin 60,
http://linkedlifedata.com/resource/pubmed/chemical/DnaJ protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GrpE protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/HSP40 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases Acting on Sulfur...,
http://linkedlifedata.com/resource/pubmed/chemical/YbbN protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/dnaK protein, E coli
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jun
|
|
pubmed:issn |
1083-351X
|
|
pubmed:author |
|
|
pubmed:issnType |
Electronic
|
|
pubmed:day |
3
|
|
pubmed:volume |
286
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
19459-69
|
|
pubmed:dateRevised |
2011-8-1
|
|
pubmed:meshHeading |
pubmed-meshheading:21498507-Amino Acid Motifs,
pubmed-meshheading:21498507-Chaperonin 60,
pubmed-meshheading:21498507-Crystallography, X-Ray,
pubmed-meshheading:21498507-Enzyme Inhibitors,
pubmed-meshheading:21498507-Escherichia coli,
pubmed-meshheading:21498507-Escherichia coli Proteins,
pubmed-meshheading:21498507-HSP40 Heat-Shock Proteins,
pubmed-meshheading:21498507-HSP70 Heat-Shock Proteins,
pubmed-meshheading:21498507-Heat-Shock Proteins,
pubmed-meshheading:21498507-Molecular Chaperones,
pubmed-meshheading:21498507-Oxidoreductases Acting on Sulfur Group Donors,
pubmed-meshheading:21498507-Protein Structure, Tertiary
|
|
pubmed:year |
2011
|
|
pubmed:articleTitle |
Escherichia coli thioredoxin-like protein YbbN contains an atypical tetratricopeptide repeat motif and is a negative regulator of GroEL.
|
|
pubmed:affiliation |
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588-0664, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
|
