Pseudouridine Synthases

Chem Biol. 2006 Nov;13(11):1125-35. doi: 10.1016/j.chembiol.2006.09.009.

Abstract

Pseudouridine synthases are the enzymes responsible for the most abundant posttranscriptional modification of cellular RNAs. These enzymes catalyze the site-specific isomerization of uridine residues that are already part of an RNA chain, and appear to employ both sequence and structural information to achieve site specificity. Crystallographic analyses have demonstrated that all pseudouridine synthases share a common core fold and active site structure and that this core is modified by peripheral domains, accessory proteins, and guide RNAs to give rise to remarkable substrate versatility.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Catalysis
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / metabolism
  • Hydro-Lyases / chemistry*
  • Hydro-Lyases / metabolism
  • Intramolecular Lyases / chemistry*
  • Intramolecular Lyases / metabolism
  • Microtubule-Associated Proteins / chemistry
  • Protein Conformation
  • Pseudouridine / chemistry*
  • Pseudouridine / metabolism
  • RNA / metabolism
  • RNA Processing, Post-Transcriptional
  • Ribonucleoproteins, Small Nuclear / chemistry
  • Ribonucleoproteins, Small Nucleolar / chemistry
  • Saccharomyces cerevisiae Proteins / chemistry

Substances

  • Escherichia coli Proteins
  • Microtubule-Associated Proteins
  • Ribonucleoproteins, Small Nuclear
  • Ribonucleoproteins, Small Nucleolar
  • Saccharomyces cerevisiae Proteins
  • Pseudouridine
  • RNA
  • Hydro-Lyases
  • CBF5 protein, S cerevisiae
  • pseudouridylate synthetase
  • Intramolecular Lyases