Abstract
Two hundred forty-five consecutive amino acids of the sigma 70 subunit of Escherichia coli RNA polymerase are not conserved in the homologous protein of Bacillus subtilis. We show that their deletion from a sigma 70-32 hybrid protein caused no severe loss of function in vivo, while sigma 70 itself retained considerable function in vitro.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacillus subtilis / enzymology
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Bacillus subtilis / genetics
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Base Sequence
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DNA-Directed RNA Polymerases / genetics*
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DNA-Directed RNA Polymerases / metabolism
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Escherichia coli / enzymology
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Escherichia coli / genetics*
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Heat-Shock Proteins / metabolism
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Molecular Sequence Data
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Sequence Deletion*
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Sigma Factor / genetics*
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Sigma Factor / metabolism
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Transcription Factors*
Substances
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Heat-Shock Proteins
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Sigma Factor
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Transcription Factors
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heat-shock sigma factor 32
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RNA polymerase sigma 70
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DNA-Directed RNA Polymerases