Source:http://linkedlifedata.com/resource/pubmed/id/10458167
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6745
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pubmed:dateCreated |
1999-9-8
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pubmed:abstractText |
The role of molecular chaperones in assisting the folding of newly synthesized proteins in the cytosol is poorly understood. In Escherichia coli, GroEL assists folding of only a minority of proteins and the Hsp70 homologue DnaK is not essential for protein folding or cell viability at intermediate growth temperatures. The major protein associated with nascent polypeptides is ribosome-bound trigger factor, which displays chaperone and prolyl isomerase activities in vitro. Here we show that delta tig::kan mutants lacking trigger factor have no defects in growth or protein folding. However, combined delta tig::kan and delta dnaK mutations cause synthetic lethality. Depletion of DnaK in the delta tig::kan mutant results in massive aggregation of cytosolic proteins. In delta tig::kan cells, an increased amount of newly synthesized proteins associated transiently with DnaK. These findings show in vivo activity for a ribosome-associated chaperone, trigger factor, in general protein folding, and functional cooperation of this protein with a cytosolic Hsp70. Trigger factor and DnaK cooperate to promote proper folding of a variety of E. coli proteins, but neither is essential for folding and viability at intermediate growth temperatures.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chaperonin 60,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Kanamycin,
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidylprolyl Isomerase,
http://linkedlifedata.com/resource/pubmed/chemical/dnaK protein, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0028-0836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
400
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
693-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10458167-Anti-Bacterial Agents,
pubmed-meshheading:10458167-Bacterial Proteins,
pubmed-meshheading:10458167-Chaperonin 60,
pubmed-meshheading:10458167-Drug Resistance,
pubmed-meshheading:10458167-Escherichia coli,
pubmed-meshheading:10458167-Escherichia coli Proteins,
pubmed-meshheading:10458167-HSP70 Heat-Shock Proteins,
pubmed-meshheading:10458167-Kanamycin,
pubmed-meshheading:10458167-Luciferases,
pubmed-meshheading:10458167-Mutation,
pubmed-meshheading:10458167-Peptidylprolyl Isomerase,
pubmed-meshheading:10458167-Protein Folding
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pubmed:year |
1999
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pubmed:articleTitle |
Trigger factor and DnaK cooperate in folding of newly synthesized proteins.
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pubmed:affiliation |
Institut für Biochemie und Molekularbiologie, Freiburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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