Literature DB >> 18955140

Structural organization of the RNA-degrading exosome.

Esben Lorentzen1, Jérôme Basquin, Elena Conti.   

Abstract

The RNA exosome participates in the degradation and processing of a wide range of RNA molecules. Recent advances in understanding how the exosome is organized and functions largely stem from structural studies. Crystal structures of archaeal exosomes bound to RNA and of the corresponding nine-subunit human exosome core show that the archaeal and eukaryotic complexes have a similar molecular architecture, but have a diverged catalytic mechanism. The crystal structures of two hydrolytic RNases that associate with the exosome provide the framework for their catalytic activity. Negative-stain EM reconstructions give us a first glimpse of how they associate with the core complex. Together, these structural studies have implications for the mechanism of RNA recruitment and degradation by the exosome complexes.

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Year:  2008        PMID: 18955140     DOI: 10.1016/j.sbi.2008.10.004

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  26 in total

1.  The human core exosome interacts with differentially localized processive RNases: hDIS3 and hDIS3L.

Authors:  Rafal Tomecki; Maiken S Kristiansen; Søren Lykke-Andersen; Aleksander Chlebowski; Katja M Larsen; Roman J Szczesny; Karolina Drazkowska; Agnieszka Pastula; Jens S Andersen; Piotr P Stepien; Andrzej Dziembowski; Torben Heick Jensen
Journal:  EMBO J       Date:  2010-06-08       Impact factor: 11.598

2.  Rrp6 is recruited to transcribed genes and accompanies the spliced mRNA to the nuclear pore.

Authors:  Viktoria Hessle; Anne von Euler; Ernesto González de Valdivia; Neus Visa
Journal:  RNA       Date:  2012-06-28       Impact factor: 4.942

3.  Structural analysis reveals the characteristic features of Mtr4, a DExH helicase involved in nuclear RNA processing and surveillance.

Authors:  John R Weir; Fabien Bonneau; Jendrik Hentschel; Elena Conti
Journal:  Proc Natl Acad Sci U S A       Date:  2010-06-21       Impact factor: 11.205

4.  Yeast nuclear RNA processing.

Authors:  Jade Bernstein; Eric A Toth
Journal:  World J Biol Chem       Date:  2012-01-26

Review 5.  mRNA quality control pathways in Saccharomyces cerevisiae.

Authors:  Satarupa Das; Biswadip Das
Journal:  J Biosci       Date:  2013-09       Impact factor: 1.826

6.  Unique properties of the Mtr4p-poly(A) complex suggest a role in substrate targeting.

Authors:  Jade Bernstein; Jeff D Ballin; Dimeka N Patterson; Gerald M Wilson; Eric A Toth
Journal:  Biochemistry       Date:  2010-11-19       Impact factor: 3.162

7.  S1 and KH domains of polynucleotide phosphorylase determine the efficiency of RNA binding and autoregulation.

Authors:  Alexander G Wong; Kristina L McBurney; Katharine J Thompson; Leigh M Stickney; George A Mackie
Journal:  J Bacteriol       Date:  2013-03-01       Impact factor: 3.490

8.  Drosophila melanogaster Dis3 N-terminal domains are required for ribonuclease activities, nuclear localization and exosome interactions.

Authors:  Megan Mamolen; Alexandra Smith; Erik D Andrulis
Journal:  Nucleic Acids Res       Date:  2010-04-26       Impact factor: 16.971

9.  The exosome associates cotranscriptionally with the nascent pre-mRNP through interactions with heterogeneous nuclear ribonucleoproteins.

Authors:  Viktoria Hessle; Petra Björk; Marcus Sokolowski; Ernesto González de Valdivia; Rebecca Silverstein; Konstantin Artemenko; Anu Tyagi; Gianluca Maddalo; Leopold Ilag; Roger Helbig; Roman A Zubarev; Neus Visa
Journal:  Mol Biol Cell       Date:  2009-06-03       Impact factor: 4.138

10.  Crystal structure of Escherichia coli polynucleotide phosphorylase core bound to RNase E, RNA and manganese: implications for catalytic mechanism and RNA degradosome assembly.

Authors:  Salima Nurmohamed; Bhamini Vaidialingam; Anastasia J Callaghan; Ben F Luisi
Journal:  J Mol Biol       Date:  2009-03-24       Impact factor: 5.469

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