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

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.

Hederstedt, LarsLund University,Lunds universitet,Molekylär cellbiologi,Biologiska institutionen,Naturvetenskapliga fakulteten,Molecular Cell Biology,Department of Biology,Faculty of Science(Swepub:lu)mikb-lhe (author)
Gamini Kannangara, CCarlsberg Research Center / Carlsberg Laboratory (author)
Gough, S. P.Carlsberg Research Center / Carlsberg Laboratory (author)
Molekylär cellbiologiBiologiska institutionen (creator_code:org_t)

By the author/editor: Schröder, Ingrid; Hederstedt, Lars; Gamini Kannangar ...; Gough, S. P.

About the subject

NATURAL SCIENCES: NATURAL SCIENCES; and Biological Scien ...; and Microbiology

NATURAL SCIENCES: NATURAL SCIENCES; and Biological Scien ...; and Biochemistry and ...

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