Challenges in RNase P Substrate Recognition: Considering the Biological Context
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.
KeywordstRNA Gene Leader Sequence Enzyme Substrate Substrate Recognition Observe Rate Constant
- Cleland WW, Cook PF (2007) Enzyme Kinetics and Mechanism. Garland Publishers, London and New YorkGoogle Scholar
- Kirsebom LA (2007). RNase P RNA mediated cleavage: Substrate recognition and catalysis. BiochimieGoogle Scholar
- Zahler NH, Sun L, et al (2005) The pre-tRNA nucleotide base and 2′-hydroxyl at N(-1) contribute to fidelity in tRNA processing by RNase P. J Mol Biol 345(5): 969–985. Epub 2004 Dec 8Google Scholar