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Interaction between the CheY response regulator and the histidine‐containing phosphotransfer (HPt) domain of the ArcB sensory kinase in Escherichia coli
Author(s) -
Yaku Hidenobu,
Kato Masato,
Hakoshima Toshio,
Tsuzuki Masakatsu,
Mizuno Takeshi
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00459-6
Subject(s) - response regulator , escherichia coli , regulator , histidine , domain (mathematical analysis) , kinase , histidine kinase , chemistry , biochemistry , biology , microbiology and biotechnology , enzyme , bacterial protein , gene , mathematical analysis , mathematics
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.