Glutamyl-tRNA reductase activity in Bacillus subtilis is dependent on the hemA gene product
(1992) In Biochemical Journal p.843-850- Abstract
- The Bacillus subtilis hemAXCDBL operon encodes enzymes for the synthesis of 5-aminolaevulinic acid via the C5 pathway (hemA and hemL) and uroporphyrinogen III (hemB, hemC and hemD). B. subtilis HemA protein (molecular mass 50 kDa) was overexpressed in hemA mutants of both Escherichia coli and B. subtilis. A mutant B. subtilis HemA protein with a Cys to Tyr change at position 105 was also overexpressed. Both wild-type and mutant HemA proteins migrated as oligomers (molecular mass greater-than-or-equal-to 230 kDa) on gel-filtration columns. All column fractions containing wild-type HemA protein had glutamyl-tRNA reductase activity. No glutamyl-tRNA reductase activity was found with the mutant HemA protein. It is concluded that the B.... (More)
- The Bacillus subtilis hemAXCDBL operon encodes enzymes for the synthesis of 5-aminolaevulinic acid via the C5 pathway (hemA and hemL) and uroporphyrinogen III (hemB, hemC and hemD). B. subtilis HemA protein (molecular mass 50 kDa) was overexpressed in hemA mutants of both Escherichia coli and B. subtilis. A mutant B. subtilis HemA protein with a Cys to Tyr change at position 105 was also overexpressed. Both wild-type and mutant HemA proteins migrated as oligomers (molecular mass greater-than-or-equal-to 230 kDa) on gel-filtration columns. All column fractions containing wild-type HemA protein had glutamyl-tRNA reductase activity. No glutamyl-tRNA reductase activity was found with the mutant HemA protein. It is concluded that the B. subtilis hemA gene product is identical to, or part of, the glutamyl-tRNA reductase of the C5 pathway. (Less)
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https://lup.lub.lu.se/record/1cd3020a-baf9-4c99-96a8-913f5856b41e
- author
- Schröder, Ingrid LU ; Hederstedt, Lars LU ; Gamini Kannangara, C and Gough, S. P.
- organization
- publishing date
- 1992
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biochemical Journal
- pages
- 843 - 850
- publisher
- Portland Press
- external identifiers
-
- scopus:0026528899
- ISSN
- 0264-6021
- DOI
- 10.1042/bj2810843
- language
- English
- LU publication?
- yes
- id
- 1cd3020a-baf9-4c99-96a8-913f5856b41e
- date added to LUP
- 2017-07-18 10:34:37
- date last changed
- 2021-01-03 08:18:22
@article{1cd3020a-baf9-4c99-96a8-913f5856b41e, abstract = {{The Bacillus subtilis hemAXCDBL operon encodes enzymes for the synthesis of 5-aminolaevulinic acid via the C5 pathway (hemA and hemL) and uroporphyrinogen III (hemB, hemC and hemD). B. subtilis HemA protein (molecular mass 50 kDa) was overexpressed in hemA mutants of both Escherichia coli and B. subtilis. A mutant B. subtilis HemA protein with a Cys to Tyr change at position 105 was also overexpressed. Both wild-type and mutant HemA proteins migrated as oligomers (molecular mass greater-than-or-equal-to 230 kDa) on gel-filtration columns. All column fractions containing wild-type HemA protein had glutamyl-tRNA reductase activity. No glutamyl-tRNA reductase activity was found with the mutant HemA protein. It is concluded that the B. subtilis hemA gene product is identical to, or part of, the glutamyl-tRNA reductase of the C5 pathway.}}, author = {{Schröder, Ingrid and Hederstedt, Lars and Gamini Kannangara, C and Gough, S. P.}}, issn = {{0264-6021}}, language = {{eng}}, pages = {{843--850}}, publisher = {{Portland Press}}, series = {{Biochemical Journal}}, title = {{Glutamyl-tRNA reductase activity in <em>Bacillus subtilis</em> is dependent on the hemA gene product}}, url = {{http://dx.doi.org/10.1042/bj2810843}}, doi = {{10.1042/bj2810843}}, year = {{1992}}, }