Interaction between the CheY response regulator and the histidine-containing phosphotransfer (HPt) domain of the ArcB sensory kinase in Escherichia coli

Hidenobu Yaku, Masato Kato, Toshio Hakoshima, Masakatsu Tsuzuki, Takeshi Mizuno

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

Bacteria have devised sophisticated His-Asp phosphorelay signaling systems for eliciting a variety of adaptive responses to their environment. The histidine-containing phosphotransfer (HPt) domain, found in many signal transduction protein, functions as a mediator of the His-Asp phosphorelay. The ArcB anaerobic sensor of E. coli contains such a HPt domain, although its function is not fully understood. In this study, we provide in vivo and in vitro evidence that the HPt domain is capable of interacting with the CheY receiver, which contains a phospho-accepting aspartate residue.

Original languageEnglish (US)
Pages (from-to)337-340
Number of pages4
JournalFEBS Letters
Volume408
Issue number3
DOIs
StatePublished - May 26 1997

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Histidine
Escherichia coli
Phosphotransferases
Signal transduction
Aspartic Acid
Signal Transduction
Bacteria
Sensors
Proteins

Keywords

  • ArcB anerobic sensor
  • CheY response regulator
  • HPt phosphotransfer domain
  • Phosphotransfer signaling in E. coli

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Interaction between the CheY response regulator and the histidine-containing phosphotransfer (HPt) domain of the ArcB sensory kinase in Escherichia coli. / Yaku, Hidenobu; Kato, Masato; Hakoshima, Toshio; Tsuzuki, Masakatsu; Mizuno, Takeshi.

In: FEBS Letters, Vol. 408, No. 3, 26.05.1997, p. 337-340.

Research output: Contribution to journalArticle

Yaku, Hidenobu ; Kato, Masato ; Hakoshima, Toshio ; Tsuzuki, Masakatsu ; Mizuno, Takeshi. / Interaction between the CheY response regulator and the histidine-containing phosphotransfer (HPt) domain of the ArcB sensory kinase in Escherichia coli. In: FEBS Letters. 1997 ; Vol. 408, No. 3. pp. 337-340.
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