The Propionibacterium freudenreichii hemYHBXRL gene cluster, which encodes enzymes and a regulator involved in the biosynthetic pathway from glutamate to protoheme

Y. Hashimoto, Mitsuo Yamashita, Y. Murooka

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24 Citations (Scopus)

Abstract

A clone that can complement both Escherichia coli hemB and hemL mutations was found among plasmids containing the Propionibacterium freudenreichii hemB gene, which encodes δ-aminolevulinic acid dehydratase. The regions upstream and downstream of the hemB gene were sequenced. Two open-reading frames (ORF1 and -2), which were similar to the hemY gene encoding protoporphyrinogen oxidase and the hemH gene encoding ferrochelatase from Bacillus subtilis, were found upstream of the hemB gene. ORF1 and -2 complemented the E. coli hemG mutation, defective in protoporphyrinogen oxidase, and the hemH gene respectively. Since ORF1 had no homology to hemG, the gene was designated hemY. The hemYHB genes appeared to be within the same transcription unit. Downstream from the hemB gene, three open-reading frames were found. One of these, transcribed in the same direction as the hemB gene, was identical to be the hemL gene, which encodes glutamate-1-semialdehyde 2,1-aminomutase. The other two open-reading frames, located between the hemYHB and hemT genes, were transcribed divergently, and their deduced amino acid sequences showed similarities to a membrane-bound transport protein and a transcriptional regulatory protein respectively. The two genes may thus be involved in hem transport and the regulation of hem gene expression respectively, and were tentatively named hemX and hemR. Although hemX and hemL are unlikely to be part of the same operon, hemYHBXRL are clustered on the P. freudenreichii chromosome.

Original languageEnglish
Pages (from-to)385-392
Number of pages8
JournalApplied Microbiology and Biotechnology
Volume47
Issue number4
DOIs
Publication statusPublished - 1997
Externally publishedYes

Fingerprint

Heme
Glutamic Acid
Enzymes
Genes
Protoporphyrinogen Oxidase
Gene encoding
glutamate-1-semialdehyde 2,1-aminomutase
Escherichia coli
Biosynthetic Pathways
Ferrochelatase
Porphobilinogen Synthase
Bacilli
Transcription
Chromosomes
Gene expression
Amino acids
Carrier Proteins
Plasmids
Proteins
Membranes

ASJC Scopus subject areas

  • Biotechnology
  • Microbiology
  • Bioengineering

Cite this

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title = "The Propionibacterium freudenreichii hemYHBXRL gene cluster, which encodes enzymes and a regulator involved in the biosynthetic pathway from glutamate to protoheme",
abstract = "A clone that can complement both Escherichia coli hemB and hemL mutations was found among plasmids containing the Propionibacterium freudenreichii hemB gene, which encodes δ-aminolevulinic acid dehydratase. The regions upstream and downstream of the hemB gene were sequenced. Two open-reading frames (ORF1 and -2), which were similar to the hemY gene encoding protoporphyrinogen oxidase and the hemH gene encoding ferrochelatase from Bacillus subtilis, were found upstream of the hemB gene. ORF1 and -2 complemented the E. coli hemG mutation, defective in protoporphyrinogen oxidase, and the hemH gene respectively. Since ORF1 had no homology to hemG, the gene was designated hemY. The hemYHB genes appeared to be within the same transcription unit. Downstream from the hemB gene, three open-reading frames were found. One of these, transcribed in the same direction as the hemB gene, was identical to be the hemL gene, which encodes glutamate-1-semialdehyde 2,1-aminomutase. The other two open-reading frames, located between the hemYHB and hemT genes, were transcribed divergently, and their deduced amino acid sequences showed similarities to a membrane-bound transport protein and a transcriptional regulatory protein respectively. The two genes may thus be involved in hem transport and the regulation of hem gene expression respectively, and were tentatively named hemX and hemR. Although hemX and hemL are unlikely to be part of the same operon, hemYHBXRL are clustered on the P. freudenreichii chromosome.",
author = "Y. Hashimoto and Mitsuo Yamashita and Y. Murooka",
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T1 - The Propionibacterium freudenreichii hemYHBXRL gene cluster, which encodes enzymes and a regulator involved in the biosynthetic pathway from glutamate to protoheme

AU - Hashimoto, Y.

AU - Yamashita, Mitsuo

AU - Murooka, Y.

PY - 1997

Y1 - 1997

N2 - A clone that can complement both Escherichia coli hemB and hemL mutations was found among plasmids containing the Propionibacterium freudenreichii hemB gene, which encodes δ-aminolevulinic acid dehydratase. The regions upstream and downstream of the hemB gene were sequenced. Two open-reading frames (ORF1 and -2), which were similar to the hemY gene encoding protoporphyrinogen oxidase and the hemH gene encoding ferrochelatase from Bacillus subtilis, were found upstream of the hemB gene. ORF1 and -2 complemented the E. coli hemG mutation, defective in protoporphyrinogen oxidase, and the hemH gene respectively. Since ORF1 had no homology to hemG, the gene was designated hemY. The hemYHB genes appeared to be within the same transcription unit. Downstream from the hemB gene, three open-reading frames were found. One of these, transcribed in the same direction as the hemB gene, was identical to be the hemL gene, which encodes glutamate-1-semialdehyde 2,1-aminomutase. The other two open-reading frames, located between the hemYHB and hemT genes, were transcribed divergently, and their deduced amino acid sequences showed similarities to a membrane-bound transport protein and a transcriptional regulatory protein respectively. The two genes may thus be involved in hem transport and the regulation of hem gene expression respectively, and were tentatively named hemX and hemR. Although hemX and hemL are unlikely to be part of the same operon, hemYHBXRL are clustered on the P. freudenreichii chromosome.

AB - A clone that can complement both Escherichia coli hemB and hemL mutations was found among plasmids containing the Propionibacterium freudenreichii hemB gene, which encodes δ-aminolevulinic acid dehydratase. The regions upstream and downstream of the hemB gene were sequenced. Two open-reading frames (ORF1 and -2), which were similar to the hemY gene encoding protoporphyrinogen oxidase and the hemH gene encoding ferrochelatase from Bacillus subtilis, were found upstream of the hemB gene. ORF1 and -2 complemented the E. coli hemG mutation, defective in protoporphyrinogen oxidase, and the hemH gene respectively. Since ORF1 had no homology to hemG, the gene was designated hemY. The hemYHB genes appeared to be within the same transcription unit. Downstream from the hemB gene, three open-reading frames were found. One of these, transcribed in the same direction as the hemB gene, was identical to be the hemL gene, which encodes glutamate-1-semialdehyde 2,1-aminomutase. The other two open-reading frames, located between the hemYHB and hemT genes, were transcribed divergently, and their deduced amino acid sequences showed similarities to a membrane-bound transport protein and a transcriptional regulatory protein respectively. The two genes may thus be involved in hem transport and the regulation of hem gene expression respectively, and were tentatively named hemX and hemR. Although hemX and hemL are unlikely to be part of the same operon, hemYHBXRL are clustered on the P. freudenreichii chromosome.

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