rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1997-4-16
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D50528,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D50529,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D50530,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D50531,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D85078,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/Z28649,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P00825,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P06541,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P19023,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P32978,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P42739,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P46272
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pubmed:abstractText |
The genes possibly encoding the b subunit (50 kDa) of the Cl(-)-translocating ATPase of Acetabularia acetabulum were cloned from total RNA and from poly(A)+ RNA and sequenced. The deduced amino acid sequence of the open reading frame consisted of 478 amino acids and showed high similarity to the beta subunit of chloroplast F1-ATPase. Gene fragments encoding the putative beta subunit of chloroplast F1- (273 bp) and mitochondrial F1-ATPases (332 bp) were also cloned from A. acetabulum and sequenced, respectively. The deduced amino acid sequence of the chloroplast F1-ATPase showed 92.5% identity to be primary structure of the b subunit of the Cl(-)-translocating ATPase, while the nucleotide sequences were 79.9% identical. The deduced amino acid sequence of the latter was 77.3% identical to that of the b subunit of the Cl(-)-translocating ATPase and the nucleotide sequences were 67.5% identical. By Northern analysis, these three beta-like genes were demonstrated to be transcribed with different sizes of RNA species. A putative chloroplast F1-beta fragment also hybridized with chloroplast DNA isolated from the organism.
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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 |
Mar
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pubmed:issn |
0003-9861
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
339
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
115-24
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9056241-Acetabularia,
pubmed-meshheading:9056241-Adenosine Triphosphatases,
pubmed-meshheading:9056241-Amino Acid Sequence,
pubmed-meshheading:9056241-Animals,
pubmed-meshheading:9056241-Anion Transport Proteins,
pubmed-meshheading:9056241-Bacterial Proteins,
pubmed-meshheading:9056241-Base Sequence,
pubmed-meshheading:9056241-Biological Transport, Active,
pubmed-meshheading:9056241-Genes, Plant,
pubmed-meshheading:9056241-Molecular Sequence Data,
pubmed-meshheading:9056241-Plant Proteins,
pubmed-meshheading:9056241-RNA, Messenger,
pubmed-meshheading:9056241-Rats,
pubmed-meshheading:9056241-Sequence Alignment,
pubmed-meshheading:9056241-Sequence Homology, Amino Acid,
pubmed-meshheading:9056241-Sequence Homology, Nucleic Acid,
pubmed-meshheading:9056241-Species Specificity
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pubmed:year |
1997
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pubmed:articleTitle |
The primary structure of the Cl(-)-translocating ATPase, b subunit of Acetabularia acetabulum, which belongs to the F-type ATPase family.
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pubmed:affiliation |
Faculty of Health and Welfare Science, Okayama Prefectural University, Soja, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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