The stability and dynamics of ribosomal protein L9: investigations of a molecular strut by amide proton exchange and circular dichroism

Journal of Molecular Biology
J LillemoenD W Hoffman

Abstract

Nuclear magnetic resonance and circular dichroism experiments were used to investigate the stability and dynamic aspects of ribosomal protein L9 from Bacillus stearothermophilus in solution. This unusually shaped protein, with its two widely spaced RNA-binding domains linked by a connecting helix, has been hypothesized to serve as a "molecular strut", most likely playing a role in ribosome assembly and/or maintaining the catalytically active conformation of ribosomal RNA. Protection factors for amide proton exchange were quantitatively measured in an extensive series of NMR experiments, providing probes of the stability and dynamics of localized regions of the protein. Results show that each of the two RNA-binding domains contains a highly stable core. The exposed central helix that connects the two domains is helical in solution, albeit not rigid, a result that is supported by amide proton protection factors, circular dichroism measurements, and carbon-13 and proton chemical shift index values. A conserved glycine and lysine-rich loop in the N-terminal domain is ordered and quite stable, a surprising result, since this loop had been presumed to be disordered in the original crystallographic analysis. Interestingly, the most dy...Continue Reading

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Citations

Sep 26, 2014·Europhysics Letters·Fatih YaşarUlrich H E Hansmann
Feb 27, 2003·The Journal of Biological Chemistry·Rosa FayosPatricia A Jennings
Nov 19, 2009·Biochemistry·Angeline M LyonDavid W Hoffman
Mar 16, 2013·ACS Chemical Biology·Jianting ZhengAdrian T Keatinge-Clay

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