Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis

Michael Lacelle, Miyuki Kumano, Kenji Kurita, Kunio Yamane, Peter Zuber, Michiko Nakano

Research output: Contribution to journalArticle

94 Citations (Scopus)

Abstract

A gene, hmp, which encodes a ubiquitous protein homologous to hemoglobin was isolated among genes from Bacillus subtilis that are induced under anaerobic conditions. The hmp protein belongs to the family of two-domain flavohemoproteins, homologs of which have been isolated from various organisms such as Escherichia coli, Alcaligenes eutrophus, and Saccharomyces cerevisiae. These proteins consist of an amino-terminal hemoglobin domain and a carboxy-terminal redox active site domain with potential binding sites for NAD(P)H and flavin adenine dinucleotide. The expression of hmp is strongly induced upon oxygen limitation, and the induction is dependent on a two- component regulatory pair, ResD and ResE, an anaerobic regulator, FNR, and respiratory nitrate reductase, NarGHJI. The requirement of FNR and NarGHJI for hmp expression is completely bypassed by the addition of nitrite in the culture medium, indicating that fnr is required for transcriptional activation of narGHJI, which produces nitrite, leading to induction of hmp expression. In contrast, induction of hmp was still dependent on resDE in the presence of nitrite. A defect in hmp in B. subtilis has no significant effect on anaerobic growth.

Original languageEnglish (US)
Pages (from-to)3803-3808
Number of pages6
JournalJournal of Bacteriology
Volume178
Issue number13
StatePublished - 1996
Externally publishedYes

Fingerprint

Nitrites
Bacillus subtilis
Oxygen
Hemoglobins
Genes
Alcaligenes
Nitrate Reductase
Proteins
Flavin-Adenine Dinucleotide
NAD
Transcriptional Activation
Oxidation-Reduction
Saccharomyces cerevisiae
Culture Media
Catalytic Domain
Binding Sites
Escherichia coli
Growth

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis. / Lacelle, Michael; Kumano, Miyuki; Kurita, Kenji; Yamane, Kunio; Zuber, Peter; Nakano, Michiko.

In: Journal of Bacteriology, Vol. 178, No. 13, 1996, p. 3803-3808.

Research output: Contribution to journalArticle

Lacelle, M, Kumano, M, Kurita, K, Yamane, K, Zuber, P & Nakano, M 1996, 'Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis', Journal of Bacteriology, vol. 178, no. 13, pp. 3803-3808.
Lacelle, Michael ; Kumano, Miyuki ; Kurita, Kenji ; Yamane, Kunio ; Zuber, Peter ; Nakano, Michiko. / Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis. In: Journal of Bacteriology. 1996 ; Vol. 178, No. 13. pp. 3803-3808.
@article{9734c70bdb0a46929283e9a7a7a096c4,
title = "Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis",
abstract = "A gene, hmp, which encodes a ubiquitous protein homologous to hemoglobin was isolated among genes from Bacillus subtilis that are induced under anaerobic conditions. The hmp protein belongs to the family of two-domain flavohemoproteins, homologs of which have been isolated from various organisms such as Escherichia coli, Alcaligenes eutrophus, and Saccharomyces cerevisiae. These proteins consist of an amino-terminal hemoglobin domain and a carboxy-terminal redox active site domain with potential binding sites for NAD(P)H and flavin adenine dinucleotide. The expression of hmp is strongly induced upon oxygen limitation, and the induction is dependent on a two- component regulatory pair, ResD and ResE, an anaerobic regulator, FNR, and respiratory nitrate reductase, NarGHJI. The requirement of FNR and NarGHJI for hmp expression is completely bypassed by the addition of nitrite in the culture medium, indicating that fnr is required for transcriptional activation of narGHJI, which produces nitrite, leading to induction of hmp expression. In contrast, induction of hmp was still dependent on resDE in the presence of nitrite. A defect in hmp in B. subtilis has no significant effect on anaerobic growth.",
author = "Michael Lacelle and Miyuki Kumano and Kenji Kurita and Kunio Yamane and Peter Zuber and Michiko Nakano",
year = "1996",
language = "English (US)",
volume = "178",
pages = "3803--3808",
journal = "Journal of Bacteriology",
issn = "0021-9193",
publisher = "American Society for Microbiology",
number = "13",

}

TY - JOUR

T1 - Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis

AU - Lacelle, Michael

AU - Kumano, Miyuki

AU - Kurita, Kenji

AU - Yamane, Kunio

AU - Zuber, Peter

AU - Nakano, Michiko

PY - 1996

Y1 - 1996

N2 - A gene, hmp, which encodes a ubiquitous protein homologous to hemoglobin was isolated among genes from Bacillus subtilis that are induced under anaerobic conditions. The hmp protein belongs to the family of two-domain flavohemoproteins, homologs of which have been isolated from various organisms such as Escherichia coli, Alcaligenes eutrophus, and Saccharomyces cerevisiae. These proteins consist of an amino-terminal hemoglobin domain and a carboxy-terminal redox active site domain with potential binding sites for NAD(P)H and flavin adenine dinucleotide. The expression of hmp is strongly induced upon oxygen limitation, and the induction is dependent on a two- component regulatory pair, ResD and ResE, an anaerobic regulator, FNR, and respiratory nitrate reductase, NarGHJI. The requirement of FNR and NarGHJI for hmp expression is completely bypassed by the addition of nitrite in the culture medium, indicating that fnr is required for transcriptional activation of narGHJI, which produces nitrite, leading to induction of hmp expression. In contrast, induction of hmp was still dependent on resDE in the presence of nitrite. A defect in hmp in B. subtilis has no significant effect on anaerobic growth.

AB - A gene, hmp, which encodes a ubiquitous protein homologous to hemoglobin was isolated among genes from Bacillus subtilis that are induced under anaerobic conditions. The hmp protein belongs to the family of two-domain flavohemoproteins, homologs of which have been isolated from various organisms such as Escherichia coli, Alcaligenes eutrophus, and Saccharomyces cerevisiae. These proteins consist of an amino-terminal hemoglobin domain and a carboxy-terminal redox active site domain with potential binding sites for NAD(P)H and flavin adenine dinucleotide. The expression of hmp is strongly induced upon oxygen limitation, and the induction is dependent on a two- component regulatory pair, ResD and ResE, an anaerobic regulator, FNR, and respiratory nitrate reductase, NarGHJI. The requirement of FNR and NarGHJI for hmp expression is completely bypassed by the addition of nitrite in the culture medium, indicating that fnr is required for transcriptional activation of narGHJI, which produces nitrite, leading to induction of hmp expression. In contrast, induction of hmp was still dependent on resDE in the presence of nitrite. A defect in hmp in B. subtilis has no significant effect on anaerobic growth.

UR - http://www.scopus.com/inward/record.url?scp=0029967350&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029967350&partnerID=8YFLogxK

M3 - Article

C2 - 8682784

AN - SCOPUS:0029967350

VL - 178

SP - 3803

EP - 3808

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 13

ER -