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PMID: 9852058 Published · ppublish English Journal Article

Regulation of the Salmonella typhimurium flavohemoglobin gene. A new pathway for bacterial gene expression in response to nitric oxide.

The Journal of biological chemistry ·Vol. 273 ·No. 51 ·1998-12-18 ·Pages 34028-32

Crawford MJ, Goldberg DE

Abstract

Flavohemoglobins, a family of two-domain proteins with homology to vertebrate hemoglobins, are found in a variety of prokaryotic and eukaryotic microorganisms. Recent studies suggest a role for these proteins in nitrogen oxide metabolism. We now show that nitric oxide donors positively regulate a chromosomal flavohemoglobin (hmp)/lacZ operon fusion in Salmonella typhimurium. hmp gene expression in the presence of NO. is independent of the SoxS, OxyR, and FNR transcription factors and instead relies on inactivation of the iron-dependent Fur repressor. Other Fur-repressed promoters in S. typhimurium are also activated by an NO. donor. In contrast to the wild-type strain, an hmp- mutant requires markedly lower concentrations of NO to induce the hmp/lacZ fusion, whereas its response to iron chelation is equivalent to wild type. These data unveil a new pathway for NO-dependent gene expression in S. typhimurium.

MeSH Terms
2,2'-Dipyridyl/pharmacology Bacterial Proteins/biosynthesis,genetics,metabolism DNA-Binding Proteins Escherichia coli Proteins Gene Expression Regulation, Bacterial/drug effects Glutathione/analogs & derivatives,pharmacology Hemeproteins/biosynthesis,genetics Iron-Sulfur Proteins/metabolism Nitric Oxide/pharmacology Nitric Oxide Donors/pharmacology Nitrogen Oxides Nitroso Compounds/pharmacology Operon Plasmids Promoter Regions, Genetic/drug effects Recombinant Fusion Proteins/biosynthesis Repressor Proteins/metabolism S-Nitrosoglutathione Salmonella typhimurium/drug effects,genetics,growth & development Spermine/analogs & derivatives,pharmacology Trans-Activators Transcription Factors/metabolism
Chemicals
Bacterial Proteins DNA-Binding Proteins Escherichia coli Proteins FNR protein, E coli Hemeproteins Iron-Sulfur Proteins Nitric Oxide Donors Nitrogen Oxides Nitroso Compounds Recombinant Fusion Proteins Repressor Proteins Trans-Activators Transcription Factors ferric uptake regulating proteins, bacterial flavohemoprotein, Bacteria spermine nitric oxide complex SoxS protein, E coli Spermine Nitric Oxide 2,2'-Dipyridyl S-Nitrosoglutathione Glutathione
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Crawford M J
Howard Hughes Medical Institute, Departments of Medicine and Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Goldberg D E
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1998-12-18
Pages
34028-32
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Corrections
ErratumIn
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