Source:http://linkedlifedata.com/resource/pubmed/id/18312274
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2008-3-12
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pubmed:abstractText |
The cmp operon of the cyanobacterium Synechococcus elongatus strain PCC 7942, encoding the subunits of the ABC-type bicarbonate transporter, is activated under CO2-limited growth conditions in a manner dependent on CmpR, a LysR family transcription factor of CbbR subfamily. The 0.7 kb long regulatory region of the operon carried a single promoter, which responded to CO2 limitation. Using the luxAB reporter system, three cis-acting elements involved in the low-CO2 activation of transcription, each consisting of a pair of LysR recognition signatures overlapping at their ends, were identified in the regulatory region. CmpR was shown to bind to the regulatory region, yielding several DNA-protein complexes in gel shift assays. Addition of ribulose-1,5-bisphosphate (> 1 mM) or 2-phosphoglycolate (> 10 microM) enhanced the binding of CmpR in a concentration-dependent manner, promoting formation of large DNA-protein complexes. Given the involvement of O2 in adaptive responses of cyanobacteria to low-CO2 conditions, our results suggest that 2-phosphoglycolate, which is produced by oxygenation by ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) of ribulose-1,5-bisphosphate under CO2-limited conditions, acts as the co-inducer in the activation of the cmp operon by CmpR.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2-phosphoglycerate,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bicarbonates,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Dioxide,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glyceric Acids,
http://linkedlifedata.com/resource/pubmed/chemical/cmpR protein, Synechococcus
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1365-2958
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
68
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
98-109
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pubmed:meshHeading |
pubmed-meshheading:18312274-Bacterial Proteins,
pubmed-meshheading:18312274-Base Sequence,
pubmed-meshheading:18312274-Bicarbonates,
pubmed-meshheading:18312274-Carbon Dioxide,
pubmed-meshheading:18312274-DNA-Binding Proteins,
pubmed-meshheading:18312274-Electrophoretic Mobility Shift Assay,
pubmed-meshheading:18312274-Gene Expression Regulation, Bacterial,
pubmed-meshheading:18312274-Glyceric Acids,
pubmed-meshheading:18312274-Molecular Sequence Data,
pubmed-meshheading:18312274-Operon,
pubmed-meshheading:18312274-Protein Binding,
pubmed-meshheading:18312274-Synechococcus,
pubmed-meshheading:18312274-Transcription, Genetic
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pubmed:year |
2008
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pubmed:articleTitle |
Mechanism of low CO2-induced activation of the cmp bicarbonate transporter operon by a LysR family protein in the cyanobacterium Synechococcus elongatus strain PCC 7942.
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pubmed:affiliation |
Laboratory of Molecular Plant Physiology, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya 464-8601, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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