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


  • eng

Conference Location

  • United States