Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1997-8-7
pubmed:databankReference
pubmed:abstractText
The Rhodobacter capsulatus sucA, sucB, and lpd genes, which encode the alpha-ketoglutarate dehydrogenase (E1o), the dihydrolipoamide succinyltransferase (E2o), and the dihydrolipoamide dehydrogenase (E3) components of the alpha-ketoglutarate dehydrogenase complex (KGD), respectively, were cloned, sequenced, and used for regulatory analyses. The KGD enzymatic activity was greater in cells grown under aerobic, respiratory growth conditions than under anaerobic, photosynthetic conditions. Similarly, the sucA gene was transcribed differentially, leading to a greater accumulation of sucA mRNAs under respiratory growth conditions than under photosynthetic conditions, although differential rates of mRNA decay could also contribute to the different amounts of sucA mRNAs under these two growth conditions. The sucA promoter was located about 4 kb upstream of the 5' end of the sucA gene, and transcripts greater than 9.5 kb hybridized to a sucA probe, suggesting the presence of an operon that produces a polycistronic mRNA. Thus, these genes seem to be expressed as an unstable primary transcript, and we speculate that posttranscriptional processes control the stoichiometry of KGD proteins.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-1103769, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-1547494, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-1692716, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-1902212, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-1995590, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-216663, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-2404759, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-2448296, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-2449287, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-2492501, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-2500417, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-2515251, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-2792374, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-2853689, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-2985470, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-2987994, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-3153191, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-3332998, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-3507689, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-3897791, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-518835, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-6187001, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-6290332, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-6294463, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-6312838, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-6339477, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-678017, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-6855607, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-6997493, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-7298578, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-7819230, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-8450304, http://linkedlifedata.com/resource/pubmed/commentcorrection/9226266-879805
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9193
pubmed:author
pubmed:issnType
Print
pubmed:volume
179
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4559-66
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:9226266-Acyltransferases, pubmed-meshheading:9226266-Amino Acid Sequence, pubmed-meshheading:9226266-Cloning, Molecular, pubmed-meshheading:9226266-Dihydrolipoamide Dehydrogenase, pubmed-meshheading:9226266-Gene Expression Regulation, Bacterial, pubmed-meshheading:9226266-Genes, Bacterial, pubmed-meshheading:9226266-Genetic Complementation Test, pubmed-meshheading:9226266-Ketoglutarate Dehydrogenase Complex, pubmed-meshheading:9226266-Molecular Sequence Data, pubmed-meshheading:9226266-Operon, pubmed-meshheading:9226266-Oxygen, pubmed-meshheading:9226266-Protein Biosynthesis, pubmed-meshheading:9226266-RNA, Messenger, pubmed-meshheading:9226266-Recombinant Fusion Proteins, pubmed-meshheading:9226266-Recombination, Genetic, pubmed-meshheading:9226266-Rhodobacter capsulatus, pubmed-meshheading:9226266-Transcription, Genetic
pubmed:year
1997
pubmed:articleTitle
Cloning, sequencing, and oxygen regulation of the Rhodobacter capsulatus alpha-ketoglutarate dehydrogenase operon.
pubmed:affiliation
Department of Microbiology, University of British Columbia, Vancouver, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't