PMID:2066329
Citation |
Squires, CL, Pedersen, S, Ross, BM and Squires, C (1991) ClpB is the Escherichia coli heat shock protein F84.1. J. Bacteriol. 173:4254-62 |
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Abstract |
ClpB is thought to be involved in proteolysis because of its sequence similarity to the ClpA subunit of the ClpA-ClpP protease. It has recently been shown that ClpP is a heat shock protein. Here we show that ClpB is the Escherichia coli heat shock protein F84.1. The F84.1 protein was overproduced in strains containing the clpB gene on a plasmid and was absent from two-dimensional gels from a clpB null mutation. Besides possessing a slower growth rate at 44 degrees C, the null mutant strain had a higher rate of death at 50 degrees C. We used reverse transcription of in vivo mRNA to show that the clpB gene was expressed from a sigma 32-specific promoter consensus sequence at both 37 and 42 degrees C. We noted that the clpB+ gene also caused the appearance of a second protein spot, F68.5, on two-dimensional gels. This spot was approximately 147 amino acids smaller than F84.1 and most probably is the result of a second translational start on the clpB mRNA. F68.5 can be observed on many published two-dimensional gels of heat-induced E. coli proteins, but the original catalog of 17 heat shock proteins did not include this spot. |
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Keywords |
Base Sequence; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli Proteins; Genes, Bacterial; Genotype; Heat-Shock Proteins/genetics; Hot Temperature; Molecular Sequence Data; Mutagenesis, Insertional; Oligonucleotide Probes; Plasmids; Promoter Regions, Genetic; Restriction Mapping; Sequence Homology, Nucleic Acid |
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