Yeast Sm-like proteins function in mRNA decapping and decay
Sundaresan Tharun,
Weihai He,
Andrew E. Mayes,
Pascal Lennertz,
Jean D. Beggs and
Roy Parker ()
Additional contact information
Sundaresan Tharun: University of Arizona
Weihai He: University of Arizona
Andrew E. Mayes: Institute of Cell and Molecular Biology, University of Edinburgh, King's Buildings
Pascal Lennertz: University of Arizona
Jean D. Beggs: Institute of Cell and Molecular Biology, University of Edinburgh, King's Buildings
Roy Parker: University of Arizona
Nature, 2000, vol. 404, issue 6777, 515-518
Abstract:
Abstract One of the main mechanisms of messenger RNA degradation in eukaryotes occurs by deadenylation-dependent decapping which leads to 5′-to-3′ decay1,2. A family of Sm-like (Lsm) proteins has been identified, members of which contain the ‘Sm’ sequence motif, form a complex with U6 small nuclear RNA and are required for pre-mRNA splicing3,4,5,6,7,8,9. Here we show that mutations in seven yeast Lsm proteins (Lsm1–Lsm7) also lead to inhibition of mRNA decapping. In addition, the Lsm1–Lsm7 proteins co-immunoprecipitate with the mRNA decapping enzyme (Dcp1), a decapping activator (Pat1/Mrt1) and with mRNA. This indicates that the Lsm proteins may promote decapping by interactions with the mRNA and the decapping machinery. In addition, the Lsm complex that functions in mRNA decay appears to be distinct from the U6-associated Lsm complex, indicating that Lsm proteins form specific complexes that affect different aspects of mRNA metabolism.
Date: 2000
References: Add references at CitEc
Citations:
Downloads: (external link)
https://www.nature.com/articles/35006676 Abstract (text/html)
Access to the full text of the articles in this series is restricted.
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:404:y:2000:i:6777:d:10.1038_35006676
Ordering information: This journal article can be ordered from
https://www.nature.com/
DOI: 10.1038/35006676
Access Statistics for this article
Nature is currently edited by Magdalena Skipper
More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().