In vitro complementation of Bacillus subtilis and Escherichia coli 2-oxoglutarate dehydrogenase complex mutants and genetic mapping of B. subtilis citK and citM mutations
(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
- Carlsson, Peter and Hederstedt, Lars LU
- organization
- publishing date
- 1986
- type
- Contribution to journal
- publication status
- published
- subject
- in
- FEMS Microbiology Letters
- volume
- 37
- issue
- 3
- pages
- 373 - 378
- publisher
- Oxford University Press
- external identifiers
-
- scopus:0022973951
- 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
- 2021-01-03 11:37:08
@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 = {{Oxford University Press}}, 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}}, doi = {{10.1111/j.1574-6968.1986.tb01827.x}}, volume = {{37}}, year = {{1986}}, }