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 language | English (US) |
|---|---|
| Pages (from-to) | 337-340 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 408 |
| Issue number | 3 |
| DOIs | |
| State | Published - May 26 1997 |
Keywords
- ArcB anerobic sensor
- CheY response regulator
- HPt phosphotransfer domain
- Phosphotransfer signaling in E. coli
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
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Yaku, H., Kato, M., Hakoshima, T., Tsuzuki, M., & Mizuno, T. (1997). Interaction between the CheY response regulator and the histidine-containing phosphotransfer (HPt) domain of the ArcB sensory kinase in Escherichia coli. FEBS Letters, 408(3), 337-340. https://doi.org/10.1016/S0014-5793(97)00459-6