The Bacillus subtilis hemAXCDBL gene cluster, which encodes enzymes of the biosynthetic pathway from glutamate to uroporphyrinogen III
(1991) In Journal of Bacteriology 173. p.2590-2599- Abstract
- We have recently reported (M. Petricek, L. Rutberg, I. Schroder, and L. Hederstedt, J. Bacteriol. 172:2250-2258, 1990) the cloning and sequence of a Bacillus subtilis chromosomal DNA fragment containing hemA proposed to encode the NAD(P)H-dependent glutamyl-tRNA reductase of the C5 pathway for 5-aminolevulinic acid (ALA) synthesis, hemX encoding a hydrophobic protein of unknown function, and hemC encoding hydroxymethylbilane synthase. In the present communication, we report the sequences and identities of three additional hem genes located immediately downstream of hemC, namely, hemD encoding uroporphyrinogen III synthase, hemB encoding porphobilinogen synthase, and hemL encoding glutamate-1-semialdehyde 2,1-aminotransferase. The six genes... (More)
- We have recently reported (M. Petricek, L. Rutberg, I. Schroder, and L. Hederstedt, J. Bacteriol. 172:2250-2258, 1990) the cloning and sequence of a Bacillus subtilis chromosomal DNA fragment containing hemA proposed to encode the NAD(P)H-dependent glutamyl-tRNA reductase of the C5 pathway for 5-aminolevulinic acid (ALA) synthesis, hemX encoding a hydrophobic protein of unknown function, and hemC encoding hydroxymethylbilane synthase. In the present communication, we report the sequences and identities of three additional hem genes located immediately downstream of hemC, namely, hemD encoding uroporphyrinogen III synthase, hemB encoding porphobilinogen synthase, and hemL encoding glutamate-1-semialdehyde 2,1-aminotransferase. The six genes are proposed to constitute a hem operon encoding enzymes required for the synthesis of uroporphyrinogen III from glutamyl-tRNA. hemA, hemB, hemC, and hemD have all been shown to be essential for heme synthesis. However, deletion of an internal 427-bp fragment of hemL did not create a growth requirement for ALA or heme, indicating that formation of ALA from glutamate-1-semialdehyde can occur spontaneously in vivo or that this reaction may also be catalyzed by other enzymes. An analysis of B. subtilis carrying integrated plasmids or deletions-substitutions in or downstream of hemL indicates that no further genes in heme synthesis are part of the proposed hem operon. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/8001491
- author
- Hansson, Mats LU ; Rutberg, L. ; Schröder, I. and Hederstedt, Lars LU
- organization
- publishing date
- 1991
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Bacteriology
- volume
- 173
- pages
- 2590 - 2599
- publisher
- American Society for Microbiology
- external identifiers
-
- scopus:0025765503
- ISSN
- 0021-9193
- DOI
- 10.1128/jb.173.8.2590-2599.1991
- language
- English
- LU publication?
- yes
- id
- bd53f3d7-f993-478e-bca1-5eadada5bf03 (old id 8001491)
- date added to LUP
- 2016-04-04 13:25:53
- date last changed
- 2021-10-03 03:20:59
@article{bd53f3d7-f993-478e-bca1-5eadada5bf03,
abstract = {{We have recently reported (M. Petricek, L. Rutberg, I. Schroder, and L. Hederstedt, J. Bacteriol. 172:2250-2258, 1990) the cloning and sequence of a Bacillus subtilis chromosomal DNA fragment containing hemA proposed to encode the NAD(P)H-dependent glutamyl-tRNA reductase of the C5 pathway for 5-aminolevulinic acid (ALA) synthesis, hemX encoding a hydrophobic protein of unknown function, and hemC encoding hydroxymethylbilane synthase. In the present communication, we report the sequences and identities of three additional hem genes located immediately downstream of hemC, namely, hemD encoding uroporphyrinogen III synthase, hemB encoding porphobilinogen synthase, and hemL encoding glutamate-1-semialdehyde 2,1-aminotransferase. The six genes are proposed to constitute a hem operon encoding enzymes required for the synthesis of uroporphyrinogen III from glutamyl-tRNA. hemA, hemB, hemC, and hemD have all been shown to be essential for heme synthesis. However, deletion of an internal 427-bp fragment of hemL did not create a growth requirement for ALA or heme, indicating that formation of ALA from glutamate-1-semialdehyde can occur spontaneously in vivo or that this reaction may also be catalyzed by other enzymes. An analysis of B. subtilis carrying integrated plasmids or deletions-substitutions in or downstream of hemL indicates that no further genes in heme synthesis are part of the proposed hem operon.}},
author = {{Hansson, Mats and Rutberg, L. and Schröder, I. and Hederstedt, Lars}},
issn = {{0021-9193}},
language = {{eng}},
pages = {{2590--2599}},
publisher = {{American Society for Microbiology}},
series = {{Journal of Bacteriology}},
title = {{The <em>Bacillus subtilis hemAXCDBL</em> gene cluster, which encodes enzymes of the biosynthetic pathway from glutamate to uroporphyrinogen III}},
url = {{http://dx.doi.org/10.1128/jb.173.8.2590-2599.1991}},
doi = {{10.1128/jb.173.8.2590-2599.1991}},
volume = {{173}},
year = {{1991}},
}