Genetic analysis of tellurate reduction reveals the selenate/tellurate reductase genes ynfEF and the transcriptional regulation of moeA by NsrR in Escherichia coli.
Escherichia coli
NsrR
molybdenum cofactor
tellurate reductase
transcriptional regulator
Journal
Journal of biochemistry
ISSN: 1756-2651
Titre abrégé: J Biochem
Pays: England
ID NLM: 0376600
Informations de publication
Date de publication:
29 Apr 2021
29 Apr 2021
Historique:
received:
30
06
2020
accepted:
20
10
2020
pubmed:
3
11
2020
medline:
30
7
2021
entrez:
2
11
2020
Statut:
ppublish
Résumé
Several bacteria can reduce tellurate into the less toxic elemental tellurium, but the genes responsible for this process have not yet been identified. In this study, we screened the Keio collection of single-gene knockouts of Escherichia coli responsible for decreased tellurate reduction and found that deletions of 29 genes, including those for molybdenum cofactor (Moco) biosynthesis, iron-sulphur biosynthesis, and the twin-arginine translocation pathway resulted in decreased tellurate reduction. Among the gene knockouts, deletions of nsrR, moeA, yjbB, ynbA, ydaS and yidH affected tellurate reduction more severely than those of other genes. Based on our findings, we determined that the ynfEF genes, which code for the components of the selenate reductase YnfEFGH, are responsible for tellurate reduction. Assays of several molybdoenzymes in the knockouts suggested that nsrR, yjbB, ynbA, ydaS and yidH are essential for the activities of molybdoenzymes in E. coli. Furthermore, we found that the nitric oxide sensor NsrR positively regulated the transcription of the Moco biosynthesis gene moeA. These findings provided new insights into the complexity and regulation of Moco biosynthesis in E. coli.
Identifiants
pubmed: 33136147
pii: 5951174
doi: 10.1093/jb/mvaa120
doi:
Substances chimiques
DNA-Binding Proteins
0
Escherichia coli Proteins
0
NsrR protein, E coli
0
Transcription Factors
0
Oxidoreductases
EC 1.-
selenate reductase
EC 1.97.-
MoeA protein, E coli
EC 2.8.1.-
Sulfurtransferases
EC 2.8.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
477-484Informations de copyright
© The Author(s) 2020. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.