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Molecular Insights into mRNA Polyadenylation and Deadenylation.
Liu, Junjie; Lu, Xubing; Zhang, Siyu; Yuan, Ling; Sun, Yadong.
Afiliación
  • Liu J; School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
  • Lu X; School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
  • Zhang S; School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
  • Yuan L; School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
  • Sun Y; School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
Int J Mol Sci ; 23(19)2022 Sep 20.
Article en En | MEDLINE | ID: mdl-36232288
ABSTRACT
Poly(A) tails are present on almost all eukaryotic mRNAs, and play critical roles in mRNA stability, nuclear export, and translation efficiency. The biosynthesis and shortening of a poly(A) tail are regulated by large multiprotein complexes. However, the molecular mechanisms of these protein machineries still remain unclear. Recent studies regarding the structural and biochemical characteristics of those protein complexes have shed light on the potential mechanisms of polyadenylation and deadenylation. This review summarizes the recent structural studies on pre-mRNA 3'-end processing complexes that initiate the polyadenylation and discusses the similarities and differences between yeast and human machineries. Specifically, we highlight recent biochemical efforts in the reconstitution of the active human canonical pre-mRNA 3'-end processing systems, as well as the roles of RBBP6/Mpe1 in activating the entire machinery. We also describe how poly(A) tails are removed by the PAN2-PAN3 and CCR4-NOT deadenylation complexes and discuss the emerging role of the cytoplasmic poly(A)-binding protein (PABPC) in promoting deadenylation. Together, these recent discoveries show that the dynamic features of these machineries play important roles in regulating polyadenylation and deadenylation.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas de Saccharomyces cerevisiae / Poliadenilación Límite: Humans Idioma: En Revista: Int J Mol Sci Año: 2022 Tipo del documento: Article País de afiliación: China

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas de Saccharomyces cerevisiae / Poliadenilación Límite: Humans Idioma: En Revista: Int J Mol Sci Año: 2022 Tipo del documento: Article País de afiliación: China