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Genetic Characterization of Bacillus subtilis odhA and odhB, encoding 2-oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase, respectively

Carlsson, P. and Hederstedt, Lars LU (1989) In Journal of Bacteriology 171(7). p.3667-3672
Abstract
The 2-oxoglutarate dehydrogenase complex consists of three different subenzymes, the E1o (2-oxoglutarate dehydrogenase) component, the E2o (dihydrolipoyl transsuccinylase) component, and the E3 (dihydrolipoamide dehydrogenase) component. In Bacillus subtilis, the E1o and E2o subenzymes are encoded by odhA and odhB, respectively. A plasmid with a 6.8-kilobase-pair DNA fragment containing odhA and odhB was isolated. Functional E1o and E2o are expressed from this plasmid in Escherichia coli. Antisera generated against B. subtilis E1o and E2o expressed in E. coli reacted with antigens of the same size from B. subtilis. The nucleotide sequence of odhB and the terminal part of odhA was determined. The deduced primary sequence of B. subtilis E2o... (More)
The 2-oxoglutarate dehydrogenase complex consists of three different subenzymes, the E1o (2-oxoglutarate dehydrogenase) component, the E2o (dihydrolipoyl transsuccinylase) component, and the E3 (dihydrolipoamide dehydrogenase) component. In Bacillus subtilis, the E1o and E2o subenzymes are encoded by odhA and odhB, respectively. A plasmid with a 6.8-kilobase-pair DNA fragment containing odhA and odhB was isolated. Functional E1o and E2o are expressed from this plasmid in Escherichia coli. Antisera generated against B. subtilis E1o and E2o expressed in E. coli reacted with antigens of the same size from B. subtilis. The nucleotide sequence of odhB and the terminal part of odhA was determined. The deduced primary sequence of B. subtilis E2o shows striking similarity to the corresponding E. coli protein, which made it possible to identify the lipoyl-binding lysine residue as well as catalytic histidine and aspartic acid residues. An mRNA of 4.5 kilobases hybridizing to both odhA and odhB probes was detected, indicating that odhA and odhB form an operon. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Bacteriology
volume
171
issue
7
pages
3667 - 3672
publisher
American Society for Microbiology
external identifiers
  • scopus:0024387073
ISSN
0021-9193
DOI
10.1128/jb.171.7.3667-3672.1989
language
English
LU publication?
yes
id
befc3f52-a647-4dcf-bfc6-4d7e510888b0
date added to LUP
2017-07-18 10:48:57
date last changed
2017-10-22 05:33:50
@article{befc3f52-a647-4dcf-bfc6-4d7e510888b0,
  abstract     = {The 2-oxoglutarate dehydrogenase complex consists of three different subenzymes, the E1o (2-oxoglutarate dehydrogenase) component, the E2o (dihydrolipoyl transsuccinylase) component, and the E3 (dihydrolipoamide dehydrogenase) component. In Bacillus subtilis, the E1o and E2o subenzymes are encoded by odhA and odhB, respectively. A plasmid with a 6.8-kilobase-pair DNA fragment containing odhA and odhB was isolated. Functional E1o and E2o are expressed from this plasmid in Escherichia coli. Antisera generated against B. subtilis E1o and E2o expressed in E. coli reacted with antigens of the same size from B. subtilis. The nucleotide sequence of odhB and the terminal part of odhA was determined. The deduced primary sequence of B. subtilis E2o shows striking similarity to the corresponding E. coli protein, which made it possible to identify the lipoyl-binding lysine residue as well as catalytic histidine and aspartic acid residues. An mRNA of 4.5 kilobases hybridizing to both odhA and odhB probes was detected, indicating that odhA and odhB form an operon. },
  author       = {Carlsson, P. and Hederstedt, Lars},
  issn         = {0021-9193},
  language     = {eng},
  number       = {7},
  pages        = {3667--3672},
  publisher    = {American Society for Microbiology},
  series       = {Journal of Bacteriology},
  title        = {Genetic Characterization of <em>Bacillus subtilis odhA</em> and <em>odhB</em>, encoding 2-oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase, respectively},
  url          = {http://dx.doi.org/10.1128/jb.171.7.3667-3672.1989},
  volume       = {171},
  year         = {1989},
}