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PMID: 11696331 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The DECD box putative ATPase Sub2p is an early mRNA export factor.

Current biology : CB ·Vol. 11 ·No. 21 ·2001-10-30 ·Pages 1711-5

Jensen TH, Boulay J, Rosbash M, Libri D

Abstract

Nuclear mRNA metabolism relies on the interplay between transcription, processing, and nuclear export. RNA polymerase II transcripts experience major rearrangements within the nucleus, which include alterations in the structure of the mRNA precursors as well as the addition and perhaps even removal of proteins prior to transport across the nuclear membrane. Such mRNP-remodeling steps are thought to require the activity of RNA helicases/ATPases. One such protein, the DECD box RNA-dependent ATPase Sub2p/UAP56, is involved in both early and late steps of spliceosome assembly. Here, we report a more general function of Saccharomyces cerevisiae Sub2p in mRNA nuclear export. We observe a rapid and dramatic nuclear accumulation of poly(A)(+) RNA in strains carrying mutant alleles of sub2. Strikingly, an intronless transcript, HSP104, also accumulates in nuclei, suggesting that Sub2p function is not restricted to splicing events. The HSP104 transcripts are localized in a single nuclear focus that is suggested to be at or near their site of transcription. Intriguingly, Sub2p shows strong genetic and functional interactions with the RNA polymerase II-associated DNA/DNA:RNA helicase Rad3p as well as the nuclear RNA exosome component Rrp6p, which was independently implicated in the retention of mRNAs at transcription sites. Taken together, our data suggest that Sub2p functions at an early step in the mRNA export process.

MeSH Terms
Active Transport, Cell Nucleus Adenosine Triphosphatases/genetics,metabolism Cell Nucleus/metabolism DNA Helicases/genetics Mutation RNA, Messenger/metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Transcription, Genetic
Chemicals
RNA, Messenger Saccharomyces cerevisiae Proteins Adenosine Triphosphatases RNA-dependent ATPase Rad3 protein, S cerevisiae DNA Helicases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Jensen T H
Howard Hughes Medical Institute, Department of Biology, Brandeis University, Waltham, MA 02454, USA. thj@mbio.aau.dk
Boulay J
Rosbash M
Libri D
Article Info
Journal
Current biology : CB
Abbr.
Curr Biol
ISSN
0960-9822
Published
2001-10-30
Pages
1711-5
Language
English
Region
England
NLM ID
9107782
Subset
IM
Grants
NIGMS NIH HHS · GM 23549 · United States
Corrections
ErratumIn
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