A novel transcriptional regulation mechanism in the flagellar regulon of Salmonella typhimurium

An anti-sigma factor inhibits the activity of the flagellum-specific sigma factor, σF

K. Ohnishi, K. Kutsukake, H. Suzuki, T. Iino

Research output: Contribution to journalArticle

166 Citations (Scopus)

Abstract

We have studied the molecular mechanism of the negative regulation by flgM of the late operons of the flagellar regulon of Salmonella typhimurium. A 7.8 kDa protein that was identified as the flgM gene product was purified to homogeneity; its amino-terminal sequence was identical to the deduced sequence except for the lack of the initiating methionine. The purified FlgM repressed transcription from the fliC promoter, one that is activated by the sigma factor, FliA (σF). No DNA-binding activity was detected in FlgM. Chemical cross-linking experiments showed that the purified FlgM bound to σF and disturbed its ability to form a complex with RNA potymerase core enzyme. These results indicate that FlgM is a novel type of negative regulator that probably inactivates the flagellum-specific sigma factor through direct interaction, i.e. it is an anti-sigma factor.

Original languageEnglish
Pages (from-to)3149-3157
Number of pages9
JournalMolecular Microbiology
Volume6
Issue number21
Publication statusPublished - Nov 1992
Externally publishedYes

Fingerprint

Sigma Factor
Regulon
Flagella
Salmonella typhimurium
Operon
Methionine
RNA
DNA
Enzymes
Genes
Proteins

ASJC Scopus subject areas

  • Molecular Biology
  • Microbiology

Cite this

A novel transcriptional regulation mechanism in the flagellar regulon of Salmonella typhimurium : An anti-sigma factor inhibits the activity of the flagellum-specific sigma factor, σF. / Ohnishi, K.; Kutsukake, K.; Suzuki, H.; Iino, T.

In: Molecular Microbiology, Vol. 6, No. 21, 11.1992, p. 3149-3157.

Research output: Contribution to journalArticle

@article{f8d01b9f182945cc9cee5ca8e009ad25,
title = "A novel transcriptional regulation mechanism in the flagellar regulon of Salmonella typhimurium: An anti-sigma factor inhibits the activity of the flagellum-specific sigma factor, σF",
abstract = "We have studied the molecular mechanism of the negative regulation by flgM of the late operons of the flagellar regulon of Salmonella typhimurium. A 7.8 kDa protein that was identified as the flgM gene product was purified to homogeneity; its amino-terminal sequence was identical to the deduced sequence except for the lack of the initiating methionine. The purified FlgM repressed transcription from the fliC promoter, one that is activated by the sigma factor, FliA (σF). No DNA-binding activity was detected in FlgM. Chemical cross-linking experiments showed that the purified FlgM bound to σF and disturbed its ability to form a complex with RNA potymerase core enzyme. These results indicate that FlgM is a novel type of negative regulator that probably inactivates the flagellum-specific sigma factor through direct interaction, i.e. it is an anti-sigma factor.",
author = "K. Ohnishi and K. Kutsukake and H. Suzuki and T. Iino",
year = "1992",
month = "11",
language = "English",
volume = "6",
pages = "3149--3157",
journal = "Molecular Microbiology",
issn = "0950-382X",
publisher = "Wiley-Blackwell",
number = "21",

}

TY - JOUR

T1 - A novel transcriptional regulation mechanism in the flagellar regulon of Salmonella typhimurium

T2 - An anti-sigma factor inhibits the activity of the flagellum-specific sigma factor, σF

AU - Ohnishi, K.

AU - Kutsukake, K.

AU - Suzuki, H.

AU - Iino, T.

PY - 1992/11

Y1 - 1992/11

N2 - We have studied the molecular mechanism of the negative regulation by flgM of the late operons of the flagellar regulon of Salmonella typhimurium. A 7.8 kDa protein that was identified as the flgM gene product was purified to homogeneity; its amino-terminal sequence was identical to the deduced sequence except for the lack of the initiating methionine. The purified FlgM repressed transcription from the fliC promoter, one that is activated by the sigma factor, FliA (σF). No DNA-binding activity was detected in FlgM. Chemical cross-linking experiments showed that the purified FlgM bound to σF and disturbed its ability to form a complex with RNA potymerase core enzyme. These results indicate that FlgM is a novel type of negative regulator that probably inactivates the flagellum-specific sigma factor through direct interaction, i.e. it is an anti-sigma factor.

AB - We have studied the molecular mechanism of the negative regulation by flgM of the late operons of the flagellar regulon of Salmonella typhimurium. A 7.8 kDa protein that was identified as the flgM gene product was purified to homogeneity; its amino-terminal sequence was identical to the deduced sequence except for the lack of the initiating methionine. The purified FlgM repressed transcription from the fliC promoter, one that is activated by the sigma factor, FliA (σF). No DNA-binding activity was detected in FlgM. Chemical cross-linking experiments showed that the purified FlgM bound to σF and disturbed its ability to form a complex with RNA potymerase core enzyme. These results indicate that FlgM is a novel type of negative regulator that probably inactivates the flagellum-specific sigma factor through direct interaction, i.e. it is an anti-sigma factor.

UR - http://www.scopus.com/inward/record.url?scp=0026539877&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026539877&partnerID=8YFLogxK

M3 - Article

VL - 6

SP - 3149

EP - 3157

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382X

IS - 21

ER -