Abstract
The Escherichia coli surE gene is co-transcribed with pcm, encoding the L-isoaspartyl protein repair methyltransferase, and is highly conserved among both the Eubacteria and the Archaea; however, no biochemical function has yet been identified for this gene. Isoaspartyl accumulation during stationary phase was much higher in a pcm surE double mutant than in either single mutant, suggesting that the two genes may represent two parallel pathways by which E. coli can respond to protein damage. A null mutation in surE also suppressed stress-survival defects previously observed in a pcm mutant strain, providing further evidence for an interaction between the two gene products.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Acid Phosphatase*
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Aspartic Acid / metabolism*
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics*
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Bacterial 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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Genes, Bacterial*
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Mutation*
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Phenotype
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Phylogeny
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Protein D-Aspartate-L-Isoaspartate Methyltransferase
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Protein Methyltransferases / genetics*
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Protein Methyltransferases / metabolism*
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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Aspartic Acid
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Protein Methyltransferases
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Protein D-Aspartate-L-Isoaspartate Methyltransferase
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Acid Phosphatase
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umpG protein, E coli