Ribonuclease P pp 135-151 | Cite as

Challenges in RNase P Substrate Recognition: Considering the Biological Context

  • Michael Harris
  • Lindsay Yandek
Part of the Protein Reviews book series (PRON, volume 10)


Despite important advances in our understanding of the structure and function of RNase P, it can be argued that we still lack a comprehensive understanding of how the functional and biophysical properties of the enzyme are integrated into its biological function. In this Chapter, we consider recent progress in understanding the in vitro kinetics and thermodynamic properties of the enzyme in the context of its specific role in tRNA biosynthesis. In the process, we highlight several studies that point the way toward gaining an integrated perspective on RNase P substrate recognition in vitro and in vivo. Both explorations point out the potential gaps in our understanding of RNase P reaction kinetics and the substrate binding specificity that may serve as points of departure for achieving a comprehensive understanding of the function of this essential enzyme in biology.


tRNA Gene Leader Sequence Enzyme Substrate Substrate Recognition Observe Rate Constant 
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Copyright information

© Springer Science+Business Media, LLC 2010

Authors and Affiliations

  1. 1.RNA Center and Department of BiochemistryCase Western Reserve University School of MedicineClevelandUSA

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