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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1996-12-18
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pubmed:abstractText |
IbpA/B, 16 kDa heat-shock proteins were recently described as recognizing heterologous protein inclusion bodies in Escherichia coli cells; the corresponding genes formed an operon regulated by the rpoH gene product, sigma 32 protein (Burland et al (1993) Genomics 16, 551; Allen et al (1992) J Bacteriol 174, 6938; Chuang et al (1993) Gene 134, 1; Chuang and Blattner (1993) J Bacteriol 175, 5242). We have found that IbpA/Bs also recognize endogenous bacterial proteins aggregated intracellularly by heat shock. IbpA/B proteins were isolated and purified from the aggregates (the S fraction), identified by amino acid microsequencing and used as immunogen for anti-IbpA/B serum preparation. Western blotting with the serum showed that in cells growing at 30 degrees C IbpA/B were located in the bacterial outer membrane and appeared in the S fraction after heat shock. Then the cellular level of the IbpA/B proteins increased about 20-fold as estimated by densitometry of the Western blots. In the E coli rpoH strain the level of IbpA/B was higher than in wild type before the heat shock and rose to still higher levels after it. This result pointed to a regulation of ibpA/B operon by another factor, besides that of sigma 32.
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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/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/IbpA protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/IbpB protein, E coli
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pubmed:status |
MEDLINE
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pubmed:issn |
0300-9084
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
78
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
117-22
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8818220-Bacterial Proteins,
pubmed-meshheading:8818220-Cell Aggregation,
pubmed-meshheading:8818220-Cell Fractionation,
pubmed-meshheading:8818220-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8818220-Escherichia coli,
pubmed-meshheading:8818220-Escherichia coli Proteins,
pubmed-meshheading:8818220-Heat-Shock Proteins,
pubmed-meshheading:8818220-Inclusion Bodies,
pubmed-meshheading:8818220-Isoelectric Focusing,
pubmed-meshheading:8818220-Molecular Weight
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pubmed:year |
1996
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pubmed:articleTitle |
IbpA and IbpB, the new heat-shock proteins, bind to endogenous Escherichia coli proteins aggregated intracellularly by heat shock.
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pubmed:affiliation |
Department of Biochemistry, University of Gda?sk, Poland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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