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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2001-6-18
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pubmed:abstractText |
A putative regulatory protein, PhaR, which was identified in the polyhydroxyalkanoic acid synthetic locus (phaZCPR) in Paracoccus denitrificans, was investigated. The PhaR protein purified from a recombinant Escherichia coli was estimated to be 22 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, being consistent with the mass calculated from the nucleotide sequence. The molecular mass was determined to be 93 kDa by size-exclusion chromatography, suggesting that the protein formed a tetramer. A gel mobility shift assay showed that PhaR specifically bound to the intergenic region of phaC--phaP. In a cell-free protein synthesis system using E. coli S30 extract, the expression of the phaP gene was repressed by the addition of purified PhaR. These results suggest that PhaR is a DNA-binding protein and may play a role in the regulation of phaP gene expression.
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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 |
Jun
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pubmed:issn |
0378-1097
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
200
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9-15
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pubmed:dateRevised |
2009-7-17
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pubmed:meshHeading |
pubmed-meshheading:11410342-Bacterial Proteins,
pubmed-meshheading:11410342-Base Sequence,
pubmed-meshheading:11410342-Cell-Free System,
pubmed-meshheading:11410342-Conserved Sequence,
pubmed-meshheading:11410342-DNA-Binding Proteins,
pubmed-meshheading:11410342-Gene Expression Regulation, Bacterial,
pubmed-meshheading:11410342-Hydroxy Acids,
pubmed-meshheading:11410342-Hydroxybutyrates,
pubmed-meshheading:11410342-Molecular Weight,
pubmed-meshheading:11410342-Paracoccus denitrificans,
pubmed-meshheading:11410342-Polyesters,
pubmed-meshheading:11410342-Promoter Regions, Genetic,
pubmed-meshheading:11410342-Protein Binding,
pubmed-meshheading:11410342-Protein Biosynthesis,
pubmed-meshheading:11410342-Protein Structure, Quaternary,
pubmed-meshheading:11410342-Recombinant Proteins,
pubmed-meshheading:11410342-Repressor Proteins,
pubmed-meshheading:11410342-Transcription, Genetic
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pubmed:year |
2001
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pubmed:articleTitle |
PhaR, a protein of unknown function conserved among short-chain-length polyhydroxyalkanoic acids producing bacteria, is a DNA-binding protein and represses Paracoccus denitrificans phaP expression in vitro.
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pubmed:affiliation |
Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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