Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators.
Journal Article (Journal Article)
Two-component systems, sensor kinase-response regulator pairs, dominate bacterial signal transduction. Regulation is exerted by phosphorylation of an Asp in receiver domains of response regulators. Lability of the acyl phosphate linkage has limited structure determination for the active, phosphorylated forms of receiver domains. As assessed by both functional and structural criteria, beryllofluoride yields an excellent analogue of aspartyl phosphate in response regulator NtrC, a bacterial enhancer-binding protein. Beryllofluoride also appears to activate the chemotaxis, sporulation, osmosensing, and nitrate/nitrite response regulators CheY, Spo0F, OmpR, and NarL, respectively. NMR spectroscopic studies indicate that beryllofluoride will facilitate both biochemical and structural characterization of the active forms of receiver domains.
Full Text
Duke Authors
Cited Authors
- Yan, D; Cho, HS; Hastings, CA; Igo, MM; Lee, SY; Pelton, JG; Stewart, V; Wemmer, DE; Kustu, S
Published Date
- December 21, 1999
Published In
Volume / Issue
- 96 / 26
Start / End Page
- 14789 - 14794
PubMed ID
- 10611291
Pubmed Central ID
- PMC24726
International Standard Serial Number (ISSN)
- 0027-8424
Digital Object Identifier (DOI)
- 10.1073/pnas.96.26.14789
Language
- eng
Conference Location
- United States