4
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Posttranscriptional RNA Pseudouridylation

      research-article
      ,
      The Enzymes

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Pseudouridine ( Ψ) is the most abundant posttranscriptional modification in noncoding RNAs. Pseudouridines are often clustered in important regions of rRNAs (ribosomal RNAs), snRNAs (small nuclear RNAs), and tRNAs (transfer RNAs), contributing to RNA function. Pseudouridylation is governed by two independent mechanisms. The first involves single protein enzymes called pseudouridine synthases (PUSs) that alone recognize the substrate and catalyze the isomerization of uridine to pseudouridine (RNA-independent pseudouridylation). The second is an RNA-guided pseudouridylation by a family of box H/ACA RNPs (ribonucleoproteins), each of which consists of a unique RNA (box H/ACA RNA) and four common core proteins (Cbf5/NAP57/Dyskerin, Nhp2/L7Ae, Nop10, and Gar1). The RNA component serves as a guide that base pairs with the substrate RNA and directs the enzyme (Cbf5) to carry out the pseudouridylation reaction at a specific site. The crystal structures of many PUSs have been solved in numerous organisms including E. coli and human. Several partial and complete crystal structures of archaea and yeast box H/ACA RNPs are available, providing a rich source of information regarding the molecular interactions between protein components and box H/ACA RNA. Over the years, several experimental systems have been developed to study the mechanism and function of pseudouridylation. Apart from noncoding RNA pseudouridylation, recent experiments have provided evidence of mRNA pseudouridylation as well. Despite remarkable progress, there is a need to accelerate efforts in order to understand the detailed mechanisms and functions of RNA pseudouridylation.

          Related collections

          Author and article information

          Journal
          101637215
          43004
          Enzymes
          Enzymes
          The Enzymes
          0423-2607
          1874-6047
          13 November 2017
          11 March 2017
          2017
          19 November 2017
          : 41
          : 151-167
          Affiliations
          University of Rochester Medical Center, Center for RNA Biology, Rochester, NY, United States
          Author notes
          [1 ]Corresponding author: yitao_yu@ 123456urmc.rochester.edu
          Article
          PMC5694665 PMC5694665 5694665 nihpa919305
          10.1016/bs.enz.2017.02.001
          5694665
          28601221
          a4b7d05a-3a0f-4a1a-82ec-d30b562262ff
          History
          Categories
          Article

          Comments

          Comment on this article