Abstract
MhpE (4-hydroxy-2-ketovalerate aldolase) and MhpF [acetaldehyde dehydrogenase (acylating)] are responsible for the last two reactions in the 3-(3-hydroxyphenyl)propionate (3-HPP) catabolic pathway in Escherichia coli, which is homologous to the meta-cleavage pathway in Pseudomonas species. Here, we report that the MhpE aldolase is associated with the MhpF dehydrogenase and that MhpF is indispensable for the folding of MhpE. Moreover, our results suggest that the mhpF and mhpE genes are translationally coupled through a reinitiation mechanism. This reinitiation mechanism may function in ensuring that the expression of mhpE occurs only when MhpF is available for the formation of a complex.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aldehyde Oxidoreductases / genetics
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Aldehyde Oxidoreductases / metabolism*
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Aldehyde-Lyases / genetics
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Aldehyde-Lyases / metabolism*
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Base Sequence
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism*
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Gene Expression Regulation, Bacterial*
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Molecular Structure
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Mutation / genetics
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Operon / genetics
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Oxo-Acid-Lyases / genetics
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Oxo-Acid-Lyases / metabolism*
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Protein Binding
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Protein Biosynthesis / genetics
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Sequence Alignment
Substances
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Escherichia coli Proteins
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Aldehyde Oxidoreductases
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acetaldehyde dehydrogenase (acylating)
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Aldehyde-Lyases
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4-hydroxy-2-ketovalerate aldolase
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Oxo-Acid-Lyases