4.5 Review Book Chapter

Structural Studies of RNase P

期刊

ANNUAL REVIEW OF BIOPHYSICS, VOL 42
卷 42, 期 -, 页码 537-557

出版社

ANNUAL REVIEWS
DOI: 10.1146/annurev-biophys-083012-130406

关键词

ribozyme; structure; mechanism; RNA/RNA recognition; catalysis; RNA architecture

资金

  1. NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM058443] Funding Source: NIH RePORTER
  2. NIGMS NIH HHS [R01 GM058443, GM58443] Funding Source: Medline

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Ribonuclease P (RNase P) is one of the first ribozymes discovered and it is found in all phylogenetic groups. It is responsible for processing the 5' end of pre-tRNAs as well as other RNA molecules. RNase P is formed by an RNA molecule responsible for catalysis and one or more proteins. Structural studies of the proteins from different organisms, the bacterial RNA component, and a bacterial RNase P holoenzyme/tRNA complex provide insights into the mechanism of this universal ribozyme. Together with the existing wealth of biochemical information, these studies provide atomic-level information on the mechanism of RNase P and continue to expand our understanding of the structure and architecture of large RNA molecules and ribonucleoprotein complexes, the nature of catalysis by ribozymes, the structural basis of recognition of RNA by RNA molecules, and the evolution of enzymes from the prebiotic, RNA-based world to the modern world.

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