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Dcp2: an mRNA decapping enzyme that adopts many different shapes and forms.
Wurm, Jan Philip; Sprangers, Remco.
Affiliation
  • Wurm JP; Department of Biophysics I, University of Regensburg, 93053, Regensburg, Germany. Electronic address: jan-philip.wurm@biologie.uni-regensburg.de.
  • Sprangers R; Department of Biophysics I, University of Regensburg, 93053, Regensburg, Germany. Electronic address: remco.sprangers@ur.de.
Curr Opin Struct Biol ; 59: 115-123, 2019 12.
Article in En | MEDLINE | ID: mdl-31473440
ABSTRACT
Eukaryotic mRNAs contain a 5' cap structure that protects the transcript against rapid exonucleolytic degradation. The regulation of cellular mRNA levels therefore depends on a precise control of the mRNA decapping pathways. The major mRNA decapping enzyme in eukaryotic cells is Dcp2. It is regulated by interactions with several activators, including Dcp1, Edc1, and Edc3, as well as by an autoinhibition mechanism. The structural and mechanistical characterization of Dcp2 complexes has long been impeded by the high flexibility and dynamic nature of the enzyme. Here we review recent insights into the catalytically active conformation of the mRNA decapping complex, the mode of action of decapping activators and the large interactions network that Dcp2 is embedded in.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Models, Molecular / Endoribonucleases Limits: Humans Language: En Journal: Curr Opin Struct Biol Journal subject: BIOLOGIA MOLECULAR Year: 2019 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Models, Molecular / Endoribonucleases Limits: Humans Language: En Journal: Curr Opin Struct Biol Journal subject: BIOLOGIA MOLECULAR Year: 2019 Document type: Article