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Organization and regulation of the Bacillus subtilis odhAB operon, which encodes two of the subenzymes of the 2-oxoglutarate dehydrogenase complex

Resnekov, Orna; Melin, Lars; Carlsson, Peter; Mannerlöf, Marie LU ; von Gabain, Alexander and Hederstedt, Lars LU (1992) In Molecular and General Genetics p.285-296
Abstract
The primary structure of Bacillus subtilis 105 kDa 2-oxoglutarate dehydrogenase (E1o) was deduced from the nucleotide sequence of the odhA gene and confirmed by N-terminal sequence analysis. The protein is highly homologous to E1o of Azotobacter vinelandii and Escherichia coli and of bakers' yeast cells. The 5′ end of the odhAB mRNA was determined and the promoter region for the odhAB operon was localized to a 375 by DNA fragment. The cellular concentration of the 4.5 kb odhAB transcript was found to be growth stage dependent; its concentration during growth in nutrient sporulation medium decreased abruptly at the end of the exponential growth phase and it was not detectable in early stationary phase. This decrease in the cellular... (More)
The primary structure of Bacillus subtilis 105 kDa 2-oxoglutarate dehydrogenase (E1o) was deduced from the nucleotide sequence of the odhA gene and confirmed by N-terminal sequence analysis. The protein is highly homologous to E1o of Azotobacter vinelandii and Escherichia coli and of bakers' yeast cells. The 5′ end of the odhAB mRNA was determined and the promoter region for the odhAB operon was localized to a 375 by DNA fragment. The cellular concentration of the 4.5 kb odhAB transcript was found to be growth stage dependent; its concentration during growth in nutrient sporulation medium decreased abruptly at the end of the exponential growth phase and it was not detectable in early stationary phase. This decrease in the cellular concentration of the transcript is not the result of an increased rate of decay of the full-length odhAB mRNA, suggesting that transcription is down-regulated at the end of the exponential growth phase. The cellular concentration of the odhA and odhB gene products, E1o and dihydrolipoamide transsuccinylase (E2o), remains essentially constant throughout the growth curve in nutrient sporulation medium, indicating that both are rather stable proteins. In exponentially growing cells, glucose in nutrient sporulation medium repressed the cellular concentration of the odhAB mRNA, as well as that of E1o and E2o, about four-fold. This effect is most likely the result of a decreased rate of transcription from the odhAB promoter, since neither the stability nor the 5′-end of the transcript were affected by glucose in the medium. It is concluded that the cellular concentration of the 2-oxoglutarate dehydrogenase multienzyme complex (E1o and E2o) is regulated mainly at the transcriptional level. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Molecular and General Genetics
pages
285 - 296
publisher
Springer
external identifiers
  • scopus:0026662882
ISSN
1432-1874
DOI
10.1007/BF00283849
language
English
LU publication?
yes
id
01a1e09d-8a6b-4025-b369-27ccbc975936
date added to LUP
2017-07-18 10:30:48
date last changed
2017-09-03 05:25:13
@article{01a1e09d-8a6b-4025-b369-27ccbc975936,
  abstract     = {The primary structure of Bacillus subtilis 105 kDa 2-oxoglutarate dehydrogenase (E1o) was deduced from the nucleotide sequence of the odhA gene and confirmed by N-terminal sequence analysis. The protein is highly homologous to E1o of Azotobacter vinelandii and Escherichia coli and of bakers' yeast cells. The 5′ end of the odhAB mRNA was determined and the promoter region for the odhAB operon was localized to a 375 by DNA fragment. The cellular concentration of the 4.5 kb odhAB transcript was found to be growth stage dependent; its concentration during growth in nutrient sporulation medium decreased abruptly at the end of the exponential growth phase and it was not detectable in early stationary phase. This decrease in the cellular concentration of the transcript is not the result of an increased rate of decay of the full-length odhAB mRNA, suggesting that transcription is down-regulated at the end of the exponential growth phase. The cellular concentration of the odhA and odhB gene products, E1o and dihydrolipoamide transsuccinylase (E2o), remains essentially constant throughout the growth curve in nutrient sporulation medium, indicating that both are rather stable proteins. In exponentially growing cells, glucose in nutrient sporulation medium repressed the cellular concentration of the odhAB mRNA, as well as that of E1o and E2o, about four-fold. This effect is most likely the result of a decreased rate of transcription from the odhAB promoter, since neither the stability nor the 5′-end of the transcript were affected by glucose in the medium. It is concluded that the cellular concentration of the 2-oxoglutarate dehydrogenase multienzyme complex (E1o and E2o) is regulated mainly at the transcriptional level.},
  author       = {Resnekov, Orna and Melin, Lars and Carlsson, Peter and Mannerlöf, Marie and von Gabain, Alexander and Hederstedt, Lars},
  issn         = {1432-1874},
  language     = {eng},
  pages        = {285--296},
  publisher    = {Springer},
  series       = {Molecular and General Genetics},
  title        = {Organization and regulation of the <em>Bacillus subtilis odhAB</em> operon, which encodes two of the subenzymes of the 2-oxoglutarate dehydrogenase complex},
  url          = {http://dx.doi.org/10.1007/BF00283849},
  year         = {1992},
}