Dynamics of backbone conformational heterogeneity in Bacillus subtilis ribonuclease P protein

Christopher H. Henkels, Yu Chu Chang, Stacy I. Chamberlin, Terrence G. Oas

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Interconversion of protein conformations is imperative to function, as evidenced by conformational changes associated with enzyme catalytic cycles, ligand binding and post-translational modifications. In this study, we used 15N NMR relaxation experiments to probe the fast (i.e., ps-ns) and slow (i.e., μs-ms) conformational dynamics of Bacillus subtilis ribonuclease P protein (P protein) in its folded state, bound to two sulfate anions. Using the Lipari-Szabo mapping method [Andrec, M., Montelione, G. T., and Levy, R. M. (2000) J. Biomol. NMR 18, 83-100] to interpret the data, we find evidence for P protein dynamics on the μs-ms time scale in the ensemble. The residues that exhibit these slow internal motions are found in regions that have been previously identified as part of the P protein-P RNA interface. These results suggest that structural flexibility within the P protein ensemble may be important for proper RNase P holoenzyme assembly and/or catalysis.

Original languageEnglish
Pages (from-to)15062-15075
Number of pages14
JournalBiochemistry
Volume46
Issue number51
DOIs
Publication statusPublished - Dec 25 2007
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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