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Glutamyl-tRNA reductase activity in Bacillus subtilis is dependent on the hemA gene product

Schröder, Ingrid LU ; Hederstedt, Lars LU ; Gamini Kannangara, C and Gough, S. P. (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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Contribution to journal
publication status
published
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in
Biochemical Journal
pages
843 - 850
publisher
Portland Press Limited
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
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2017-08-18 11:12:55
@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 Limited},
  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},
  year         = {1992},
}