Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators
- Dalai Yan*,†,
- Ho S. Cho‡,
- Curtis A. Hastings‡,
- Michele M. Igo§,
- Seok-Yong Lee‡,¶,
- Jeffrey G. Pelton‡,
- Valley Stewart§,
- David E. Wemmer‡,‖, and
- Sydney Kustu*
- *Department of Plant and Microbial Biology, ¶Graduate Group in Biophysics, and ‖Department of Chemistry, University of California, Berkeley, CA 94720; ‡Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720; and §Section of Microbiology, University of California, Davis, CA 95616
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Contributed by Sydney Kustu
Abstract
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.
Footnotes
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↵ † To whom reprint requests should be addressed. E-mail: dyan{at}nature.berkeley.edu.
- Abbreviations:
- NtrC,
- nitrogen regulatory protein C;
- D54,
- Asp-54;
- NtrCr,
- receiver domain of NtrC;
- P-NtrCr,
- phosphorylated NtrCr;
- BeFx,
- beryllofluoride;
- VO43−,
- orthovanadate;
- NtrCWT,
- wild-type NtrC
- Copyright © 1999, The National Academy of Sciences
