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In vitro complementation of Bacillus subtilis and Escherichia coli 2-oxoglutarate dehydrogenase complex mutants and genetic mapping of B. subtilis citK and citM mutations

Carlsson, Peter and Hederstedt, Lars LU (1986) In FEMS Microbiology Letters 37(3). p.373-378
Abstract
Abstract


The 2-oxoglutarate dehydrogenase complex of the tricarboxylic acid cycle (TCA) consists of multiple copies of 3 different subenzymes; E1, E2 and E3. The E3 subenzyme is also a component of the pyruvate dehydrogenase complex. Bacillus subtilis 2-oxoglutarate dehydrogenase mutants were studied. The mutants defective in E1, E2 and E3 subenzyme activity, respectively, could be separated into 3 groups by biochemical complementation analyses. The groups correspond to the citK, citM and citL genes. A B. subtilis subenzyme defect, probably E1, could be complemented with the corresponding Escherichia coli wild-type subenzyme and vice versa. Mutations in citK and citM are closely linked. The gene order kauA--- ---citK-citM was... (More)
Abstract


The 2-oxoglutarate dehydrogenase complex of the tricarboxylic acid cycle (TCA) consists of multiple copies of 3 different subenzymes; E1, E2 and E3. The E3 subenzyme is also a component of the pyruvate dehydrogenase complex. Bacillus subtilis 2-oxoglutarate dehydrogenase mutants were studied. The mutants defective in E1, E2 and E3 subenzyme activity, respectively, could be separated into 3 groups by biochemical complementation analyses. The groups correspond to the citK, citM and citL genes. A B. subtilis subenzyme defect, probably E1, could be complemented with the corresponding Escherichia coli wild-type subenzyme and vice versa. Mutations in citK and citM are closely linked. The gene order kauA--- ---citK-citM was determined from 3-factor transformation crosses. It is concluded that the gene organization and the subenzyme structure of the 2-oxoglutarate dehydrogenase complex are similar in B. subtilis and E. coli.
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
FEMS Microbiology Letters
volume
37
issue
3
pages
373 - 378
publisher
Elsevier
ISSN
1574-6968
DOI
10.1111/j.1574-6968.1986.tb01827.x
language
English
LU publication?
yes
id
4b5a82e3-23db-4a51-8e63-10393b0a88a7
date added to LUP
2017-07-18 11:04:11
date last changed
2017-09-26 14:48:23
@article{4b5a82e3-23db-4a51-8e63-10393b0a88a7,
  abstract     = {Abstract<br/><br/><br/>The 2-oxoglutarate dehydrogenase complex of the tricarboxylic acid cycle (TCA) consists of multiple copies of 3 different subenzymes; E1, E2 and E3. The E3 subenzyme is also a component of the pyruvate dehydrogenase complex. Bacillus subtilis 2-oxoglutarate dehydrogenase mutants were studied. The mutants defective in E1, E2 and E3 subenzyme activity, respectively, could be separated into 3 groups by biochemical complementation analyses. The groups correspond to the citK, citM and citL genes. A B. subtilis subenzyme defect, probably E1, could be complemented with the corresponding Escherichia coli wild-type subenzyme and vice versa. Mutations in citK and citM are closely linked. The gene order kauA--- ---citK-citM was determined from 3-factor transformation crosses. It is concluded that the gene organization and the subenzyme structure of the 2-oxoglutarate dehydrogenase complex are similar in B. subtilis and E. coli.<br/>},
  author       = {Carlsson, Peter and Hederstedt, Lars},
  issn         = {1574-6968},
  language     = {eng},
  number       = {3},
  pages        = {373--378},
  publisher    = {Elsevier},
  series       = {FEMS Microbiology Letters},
  title        = {In vitro complementation of <em>Bacillus subtilis</em> and <em>Escherichia coli</em> 2-oxoglutarate dehydrogenase complex mutants and genetic mapping of<em> B. subtilis citK</em> and <em>citM</em> mutations},
  url          = {http://dx.doi.org/10.1111/j.1574-6968.1986.tb01827.x},
  volume       = {37},
  year         = {1986},
}