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PMID: 19060898 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities.

Nature structural & molecular biology ·Vol. 16 ·No. 1 ·2009-01-00 ·Pages 56-62

Schaeffer D, Tsanova B, Barbas A, Reis FP, Dastidar EG, Sanchez-Rotunno M, Arraiano CM, van Hoof A

Abstract

The eukaryotic exosome is a ten-subunit 3' exoribonucleolytic complex responsible for many RNA-processing and RNA-degradation reactions. How the exosome accomplishes this is unknown. Rrp44 (also known as Dis3), a member of the RNase II family of enzymes, is the catalytic subunit of the exosome. We show that the PIN domain of Rrp44 has endoribonucleolytic activity. The PIN domain is preferentially active toward RNA with a 5' phosphate, suggesting coordination of 5' and 3' processing. We also show that the endonuclease activity is important in vivo. Furthermore, the essential exosome subunit Csl4 does not contain any domains that are required for viability, but its zinc-ribbon domain is required for exosome-mediated mRNA decay. These results suggest that specific exosome domains contribute to specific functions, and that different RNAs probably interact with the exosome differently. The combination of an endoRNase and an exoRNase activity seems to be a widespread feature of RNA-degrading machines.

MeSH Terms
Animals Catalytic Domain Cytoplasm/metabolism Endoribonucleases/metabolism Exoribonucleases/metabolism Exosome Multienzyme Ribonuclease Complex Exosomes/enzymology,genetics Humans Peptide Fragments/chemistry,metabolism RNA, Messenger/chemistry,genetics,metabolism Ribonucleases/genetics,metabolism Saccharomyces cerevisiae/genetics,metabolism Saccharomyces cerevisiae Proteins/genetics,metabolism
Chemicals
Peptide Fragments RNA, Messenger Saccharomyces cerevisiae Proteins Endoribonucleases Exoribonucleases Exosome Multienzyme Ribonuclease Complex Ribonucleases DIS3 protein, S cerevisiae
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Schaeffer Daneen
Department of Microbiology and Molecular Genetics, University of Texas Health Science Center-Houston, 6431 Fannin Street, MSB 1.212 Houston, Texas 77030, USA.
Tsanova Borislava
Barbas Ana
Reis Filipa Pereira
Dastidar Eeshita Ghosh
Sanchez-Rotunno Maya
Arraiano Cecília Maria
van Hoof Ambro
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Article Info
Journal
Nature structural & molecular biology
Abbr.
Nat Struct Mol Biol
ISSN
1545-9985
Published
2009-01-00
Epub
2008-00-07
Pages
56-62
Language
English
Region
United States
NLM ID
101186374
PMCID
PMC2615074
Subset
IM
Grants
NIGMS NIH HHS · R01 GM069900-01A1 · United States
NIGMS NIH HHS · R01 GM069900-02 · United States
NIGMS NIH HHS · R01 GM069900-04 · United States
NIGMS NIH HHS · R01 GM069900-03 · United States
NIGMS NIH HHS · R01 GM069900 · United States
NIGMS NIH HHS · (GM069900 · United States
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