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PMID: 17942686 Published · ppublish English Journal Article Research Support, N.I.H., Extramural

Architecture of the yeast Rrp44 exosome complex suggests routes of RNA recruitment for 3' end processing.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 104 ·No. 43 ·2007-10-23 ·Pages 16844-9

Wang HW, Wang J, Ding F, Callahan K, Bratkowski MA, Butler JS, Nogales E, Ke A

Abstract

The eukaryotic core exosome (CE) is a conserved nine-subunit protein complex important for 3' end trimming and degradation of RNA. In yeast, the Rrp44 protein constitutively associates with the CE and provides the sole source of processive 3'-to-5' exoribonuclease activity. Here we present EM reconstructions of the core and Rrp44-bound exosome complexes. The two-lobed Rrp44 protein binds to the RNase PH domain side of the exosome and buttresses the bottom of the exosome-processing chamber. The Rrp44 C-terminal body part containing an RNase II-type active site is anchored to the exosome through a conserved set of interactions mainly to the Rrp45 and Rrp43 subunit, whereas the Rrp44 N-terminal head part is anchored to the Rrp41 subunit and may function as a roadblock to restrict access of RNA to the active site in the body region. The Rrp44-exosome (RE) architecture suggests an active site sequestration mechanism for strict control of 3' exoribonuclease activity in the RE complex.

MeSH Terms
Amino Acid Sequence Binding Sites Conserved Sequence Exoribonucleases/metabolism Exosome Multienzyme Ribonuclease Complex Humans Models, Biological Models, Molecular Molecular Sequence Data Protein Binding Protein Conformation RNA Processing, Post-Transcriptional RNA Transport RNA, Fungal/metabolism Saccharomyces cerevisiae/enzymology,metabolism Saccharomyces cerevisiae Proteins/chemistry,isolation & purification,ultrastructure Sequence Alignment Substrate Specificity
Chemicals
RNA, Fungal Saccharomyces cerevisiae Proteins Exoribonucleases Exosome Multienzyme Ribonuclease Complex DIS3 protein, S cerevisiae
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Wang Hong-Wei
Life Sciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA. [email protected]
Wang Jianjun
Ding Fang
Callahan Kevin
Bratkowski Matthew A
Butler J Scott
Nogales Eva
Ke Ailong
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.0705526104
Email
[email protected]
Published
2007-10-23
Epub
2007-00-17
Pages
16844-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC2040474
Subset
IM
Grants
NIGMS NIH HHS · R01 GM059898 · United States
NIGMS NIH HHS · GM 59898 · United States
External Links
PubMed source DOI: 10.1073/pnas.0705526104 PMC Full Text View journal details
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