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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2006-6-26
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
346
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1009-15
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16782065-Aldehyde Oxidoreductases,
pubmed-meshheading:16782065-Aldehyde-Lyases,
pubmed-meshheading:16782065-Base Sequence,
pubmed-meshheading:16782065-Escherichia coli,
pubmed-meshheading:16782065-Escherichia coli Proteins,
pubmed-meshheading:16782065-Gene Expression Regulation, Bacterial,
pubmed-meshheading:16782065-Molecular Structure,
pubmed-meshheading:16782065-Mutation,
pubmed-meshheading:16782065-Operon,
pubmed-meshheading:16782065-Oxo-Acid-Lyases,
pubmed-meshheading:16782065-Protein Binding,
pubmed-meshheading:16782065-Protein Biosynthesis,
pubmed-meshheading:16782065-Sequence Alignment
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pubmed:year |
2006
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pubmed:articleTitle |
Coupled expression of MhpE aldolase and MhpF dehydrogenase in Escherichia coli.
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pubmed:affiliation |
Department of Chemistry and Center for Molecular Design and Synthesis, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Republic of Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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