Abstract
We isolated 26 suppressor mutations that allowed growth of a delta pdxH::omega null mutant in the absence of pyridoxal. Each suppressor mapped to pdxJ, and the eight suppressors sequenced contained the same glycine-to-serine change in the PdxJ polypeptide. This bypass suppression suggests that PdxJ may participate in formation of the pyridine ring of pyridoxine 5'-phosphate.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Bacterial Proteins / genetics*
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Escherichia coli / enzymology
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Escherichia coli / genetics*
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Escherichia coli Proteins*
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Ligases*
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Models, Biological
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Mutagenesis, Insertional
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Point Mutation*
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Pyridoxal Phosphate / analogs & derivatives
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Pyridoxal Phosphate / biosynthesis*
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Pyridoxal Phosphate / metabolism
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Pyridoxaminephosphate Oxidase / genetics
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Pyridoxaminephosphate Oxidase / metabolism
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Sequence Deletion
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Suppression, Genetic*
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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PdxJ protein, E coli
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Pyridoxal Phosphate
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Pyridoxaminephosphate Oxidase
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Ligases
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pyridoxine 5-phosphate