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Cloning and characterization of the hemA region of the Bacillus subtilis chromosome

Petricek, M; Rutberg, Lars; Schröder, I. and Hederstedt, Lars LU (1990) In Journal of Bacteriology p.2250-2258
Abstract
A 3.8-kilobase DNA fragment from Bacillus subtilis containing the hemA gene has been cloned and sequenced. Four open reading frames were identified. The first is hemA, encoding a protein of 50.8 kilodaltons. The primary defect of a B. subtilis 5-aminolevulinic acid-requiring mutant was identified as a cysteine-to-tyrosine substitution in the HemA protein. The predicted amino acid sequence of the B. subtilis HemA protein showed 34% identity with the Escherichia coli HemA protein, which is known to code for the NAD(P)H:glutamyl-tRNA reductase of the C5 pathway for 5-aminolevulinic acid synthesis. The B. subtilis HemA protein also complements the defect of an E. coli hemA mutant. The second open reading frame in the cloned fragment, called... (More)
A 3.8-kilobase DNA fragment from Bacillus subtilis containing the hemA gene has been cloned and sequenced. Four open reading frames were identified. The first is hemA, encoding a protein of 50.8 kilodaltons. The primary defect of a B. subtilis 5-aminolevulinic acid-requiring mutant was identified as a cysteine-to-tyrosine substitution in the HemA protein. The predicted amino acid sequence of the B. subtilis HemA protein showed 34% identity with the Escherichia coli HemA protein, which is known to code for the NAD(P)H:glutamyl-tRNA reductase of the C5 pathway for 5-aminolevulinic acid synthesis. The B. subtilis HemA protein also complements the defect of an E. coli hemA mutant. The second open reading frame in the cloned fragment, called ORF2, codes for a protein of about 30 kilodaltons with unknown function. It is not the proposed hemB gene product porphobilinogen synthase. The third open reading frame is hemC, coding for porphobilinogen deaminase. The fourth open reading frame extends past the sequenced fragment and may be identical to hemD, coding for uroporphyrinogen III cosynthase. Analysis of deletion mutants of the hemA region suggests that (at least) hemA, ORF2, and hemC may be part of an operon. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Bacteriology
pages
2250 - 2258
publisher
American Society for Microbiology
external identifiers
  • scopus:0025318409
ISSN
0021-9193
DOI
10.1128/jb.172.5.2250-2258.1990
language
English
LU publication?
yes
id
99c288fa-1995-4ddc-a602-aa0e87517497
date added to LUP
2017-07-18 10:44:48
date last changed
2017-09-10 05:21:59
@article{99c288fa-1995-4ddc-a602-aa0e87517497,
  abstract     = {A 3.8-kilobase DNA fragment from Bacillus subtilis containing the hemA gene has been cloned and sequenced. Four open reading frames were identified. The first is hemA, encoding a protein of 50.8 kilodaltons. The primary defect of a B. subtilis 5-aminolevulinic acid-requiring mutant was identified as a cysteine-to-tyrosine substitution in the HemA protein. The predicted amino acid sequence of the B. subtilis HemA protein showed 34% identity with the Escherichia coli HemA protein, which is known to code for the NAD(P)H:glutamyl-tRNA reductase of the C5 pathway for 5-aminolevulinic acid synthesis. The B. subtilis HemA protein also complements the defect of an E. coli hemA mutant. The second open reading frame in the cloned fragment, called ORF2, codes for a protein of about 30 kilodaltons with unknown function. It is not the proposed hemB gene product porphobilinogen synthase. The third open reading frame is hemC, coding for porphobilinogen deaminase. The fourth open reading frame extends past the sequenced fragment and may be identical to hemD, coding for uroporphyrinogen III cosynthase. Analysis of deletion mutants of the hemA region suggests that (at least) hemA, ORF2, and hemC may be part of an operon. },
  author       = {Petricek, M and Rutberg, Lars and Schröder, I. and Hederstedt, Lars},
  issn         = {0021-9193},
  language     = {eng},
  pages        = {2250--2258},
  publisher    = {American Society for Microbiology},
  series       = {Journal of Bacteriology},
  title        = {Cloning and characterization of the <em>hemA</em> region of the <em>Bacillus subtilis</em> chromosome},
  url          = {http://dx.doi.org/10.1128/jb.172.5.2250-2258.1990 },
  year         = {1990},
}