Journal article
Signal transduction in chemotaxis. A propagating conformation change upon phosphorylation of CheY
The Journal of biological chemistry, Vol.269(42), pp.26358-26362
10/21/1994
Handle:
https://hdl.handle.net/2376/118044
PMID: 7929354
Abstract
The CheY protein from Escherichia coli and Salmonella typhimurium are among the best characterized proteins of the receiver domain family of two component signal transduction systems in bacteria. Phosphorylation of CheY plays a central role in bacterial chemotaxis. However, it is not entirely clear how its state of phosphorylation contributes to its function. Genetic evidence suggests that CheY changes its conformation upon phosphorylation. We present evidence for this conformation change by comparing the NMR 15N-1H correlation spectra of CheY.Mg2+ complex and phospho-CheY in the presence of magnesium. Large changes in chemical shift are used as indicators of chemical changes and probable structural changes in the protein backbone. Our observations suggest that significant structural changes occur in CheY upon phosphorylation and that these changes are distinct from the changes produced by magnesium ion binding. In addition to residues Asn-59 and Gly-65 that are immediately adjacent to the site of phosphorylation at Asp-57, a large number of other residues show significant chemical shift changes as a result of phosphorylation. These include Met-17, Val-21, Asn-23, Gly-39, Met-60, Met-63, Asp-64, Leu-66, Glu-67, Leu-68, Leu-69, Met-85, Val-86, Thr-87, Ala-88, Asn-94, Val-107, Lys-109, Thr-112, Ala-113, Ala-114, and Asn-121. These results appear inconsistent with the recent suggestion that phosphorylation produces the same structural changes as magnesium binding (Bellsolell, L., Prieto, J., Serrano, L., and Coll, M. (1994) J. Mol. Biol. 238, 489-495). We find that some regions change overlap with a genetically defined motor binding face. We therefore propose that the conformation switch modulates the interaction of CheY with its target, the flagellar motor. Other regions also change, possibly reflecting the many different functions of CheY homologues.
Metrics
12 Record Views
Details
- Title
- Signal transduction in chemotaxis. A propagating conformation change upon phosphorylation of CheY
- Creators
- D F Lowry - Institute of Molecular Biology, University of Oregon, Eugene 97403A F RothP B RupertF W DahlquistF J MoyP J DomailleP Matsumura
- Publication Details
- The Journal of biological chemistry, Vol.269(42), pp.26358-26362
- Academic Unit
- Engineering and Applied Sciences (TRIC), School of
- Publisher
- United States
- Grant note
- GM33677 / NIGMS NIH HHS AI18985 / NIAID NIH HHS
- Identifiers
- 99900548471601842
- Language
- English
- Resource Type
- Journal article