Source:http://linkedlifedata.com/resource/pubmed/id/10548510
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1999-12-17
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pubmed:databankReference | |
pubmed:abstractText |
Hydrogenovibrio marinus strain MH-110, an obligately lithoautotrophic hydrogen-oxidizing bacterium, possesses three sets of the genes for ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO): namely, two form I type (cbbLS-1 and cbbLS-2) and one form II type (cbbM) enzymes. The cbbQ-m gene was located downstream of cbbM, and showed high similarity to other cbbQ genes and nirQ/norQ genes in denitrifying bacteria. Phylogenetic analysis of CbbQ and NirQ/NorQ indicated that CbbQ-m from Hv. marinus closely resembled CbbQ from Thiobacillus intermedius and Thiobacillus neapolitannus and less closely resembled NirQ and NorQ. The cbbQ-m gene has been shown to activate the form II RubisCO in E. coli cells, and the cbbQ-t from Hydrogenophilus thermoluteolus could also activate the form II RubisCO. Both cbbQ genes have also been shown to activate the form I RubisCO from Hp. thermoluteolus in E. coli cells. However, the activation levels of two form I RubisCOs from Hv. marinus were smaller than that of form I RubisCOs from Hp. thermoluteolus. Form II RubisCO activated by CbbQ-m (QM) was purified from E. coli cells. The result of the 8-anilino-1-naphthalenesulfonate binding assay and the circular dichroism spectra indicated that QM was conformationally different from Form II RubisCO that was not activated by CbbQ.
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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/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CbbQ protein, bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Ribulose-Bisphosphate Carboxylase
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 1999 Academic Press.
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pubmed:issnType |
Print
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pubmed:volume |
265
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
177-83
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:10548510-Amino Acid Sequence,
pubmed-meshheading:10548510-Bacterial Proteins,
pubmed-meshheading:10548510-Carrier Proteins,
pubmed-meshheading:10548510-Cloning, Molecular,
pubmed-meshheading:10548510-Escherichia coli,
pubmed-meshheading:10548510-Evolution, Molecular,
pubmed-meshheading:10548510-Isoenzymes,
pubmed-meshheading:10548510-Molecular Sequence Data,
pubmed-meshheading:10548510-Phylogeny,
pubmed-meshheading:10548510-Protein Conformation,
pubmed-meshheading:10548510-Restriction Mapping,
pubmed-meshheading:10548510-Ribulose-Bisphosphate Carboxylase,
pubmed-meshheading:10548510-Sequence Alignment,
pubmed-meshheading:10548510-Sequence Homology, Amino Acid,
pubmed-meshheading:10548510-Thiobacillus,
pubmed-meshheading:10548510-Vibrionaceae
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pubmed:year |
1999
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pubmed:articleTitle |
The cbbQ genes, located downstream of the form I and form II RubisCO genes, affect the activity of both RubisCOs.
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pubmed:affiliation |
Department of Biotechnology, University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo, 113-8657, Japan.
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pubmed:publicationType |
Journal Article
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