Abstract
The DnaK chaperone of Escherichia coli is known to interact with the J domains of DnaJ, CbpA, and DjlA. By constructing multiple mutants, we found that the djlA gene was essential for bacterial growth above 37 degrees C in the absence of dnaJ. This essentiality depended upon the J domain of DjlA but not upon the normal membrane location of DjlA.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism
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Escherichia coli / genetics
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Escherichia coli / growth & development*
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Escherichia coli / metabolism
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Escherichia coli Proteins*
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HSP40 Heat-Shock Proteins
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Heat-Shock Proteins / genetics*
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Heat-Shock Proteins / metabolism*
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Hot Temperature
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Mutation
Substances
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CbpA protein, E coli
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DNA-Binding Proteins
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DjlA protein, E coli
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DnaJ protein, E coli
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Escherichia coli Proteins
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HSP40 Heat-Shock Proteins
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Heat-Shock Proteins