PMID:8349564
| Citation |
Chuang, SE and Blattner, FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J. Bacteriol. 175:5242-52 |
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| Abstract |
Most organisms respond to heat by substantial alteration of the pattern of gene expression. This has been particularly well studied with Escherichia coli although the response has by no means been completely characterized. Here we report the characterization of 26 new heat shock genes of E. coli, termed hsl, discovered by global transcription analysis with an overlapping lambda clone bank. We have measured the molecular weights of the corresponding heat shock proteins and mapped each of them to within a few kilobases on the E. coli genome. In vitro, 16 of them can be activated by the E sigma 32 RNA polymerase, which specifically transcribes heat shock genes. In vivo expression kinetics of seven of eight examined new proteins were found to be similar to those of the four most studied heat shock proteins, DnaK, DnaJ, GroEL (MopA), and GroES (MopB). In the course of this work, we confirmed that the catalytic subunit of the ATP-dependent Clp protease (also known as Ti protease), ClpP, is derived from a larger precursor protein. Possible assignments of some of the hsl genes to known proteins are discussed. |
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| Keywords |
Bacterial Proteins/biosynthesis; Bacterial Proteins/genetics; Bacteriophage lambda/genetics; Chromosome Mapping; Cloning, Molecular; Escherichia coli/genetics; Gene Expression Regulation, Bacterial; Genes, Bacterial/genetics; Heat-Shock Proteins/biosynthesis; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Recombinant Proteins/biosynthesis; Sigma Factor/metabolism; Transcription Factors; Transcription, Genetic/radiation effects; Ultraviolet Rays |
| edit table |
Significance
Chuang and Blattner dentified 26 new heat shock proteins, in addition to the 17 previously identified by Neidhardt and van Bogelen (1987).[1] Fourteen of the 26 proteins have not been associated with an E. coli gene: HslA, HslB, HslC, HslD, HslE, HslG, HslH, HslK, HslL, HslM, HslN, HslP, HslQ, and HslW.
Based on its electrophoretic behavior on 2-D gels, HslI is proposed to correspond to HtpR (pg. xx).
The fermentative lactate dehydrogenase (LdhA) has been associated with both HslI/HtpH and HslF. HslI is expressed from a Kohara clone (1E7, id=265) that also carries the ldhA gene. The apparent MW (35.6) and pI (5.59) of HtpR from 2-D gel electrophoresis[2] are similar to those calculated for LdhA (36.5 kDa and 5.2, respectively). I haven't been able to figure out how HslF came to be associated with LdhA. HslF maps to a different Kohara clone (6B4 id=260) and has an apparent MW of 51 kDa.
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