Document Detail

Both Sm-domain and C-terminal extension of Lsm1 are important for the RNA-binding activity of the Lsm1-7-Pat1 complex.
MedLine Citation:
PMID:  22450758     Owner:  NLM     Status:  MEDLINE    
Lsm proteins are a ubiquitous family of proteins characterized by the Sm-domain. They exist as hexa- or heptameric RNA-binding complexes and carry out RNA-related functions. The Sm-domain is thought to be sufficient for the RNA-binding activity of these proteins. The highly conserved eukaryotic Lsm1 through Lsm7 proteins are part of the cytoplasmic Lsm1-7-Pat1 complex, which is an activator of decapping in the conserved 5'-3' mRNA decay pathway. This complex also protects mRNA 3'-ends from trimming in vivo. Purified Lsm1-7-Pat1 complex is able to bind RNA in vitro and exhibits a unique binding preference for oligoadenylated RNA (over polyadenylated and unadenylated RNA). Lsm1 is a key subunit that determines the RNA-binding properties of this complex. The normal RNA-binding activity of this complex is crucial for mRNA decay and 3'-end protection in vivo and requires the intact Sm-domain of Lsm1. Here, we show that though necessary, the Sm-domain of Lsm1 is not sufficient for the normal RNA-binding ability of the Lsm1-7-Pat1 complex. Deletion of the C-terminal domain (CTD) of Lsm1 (while keeping the Sm-domain intact) impairs mRNA decay in vivo and results in Lsm1-7-Pat1 complexes that are severely impaired in RNA binding in vitro. Interestingly, the mRNA decay and 3'-end protection defects of such CTD-truncated lsm1 mutants could be suppressed in trans by overexpression of the CTD polypeptide. Thus, unlike most Sm-like proteins, Lsm1 uniquely requires both its Sm-domain and CTD for its normal RNA-binding function.
Ashis Chowdhury; Kalidindi K Raju; Swathi Kalurupalle; Sundaresan Tharun
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2012-03-26
Journal Detail:
Title:  RNA (New York, N.Y.)     Volume:  18     ISSN:  1469-9001     ISO Abbreviation:  RNA     Publication Date:  2012 May 
Date Detail:
Created Date:  2012-04-18     Completed Date:  2012-06-12     Revised Date:  2013-06-26    
Medline Journal Info:
Nlm Unique ID:  9509184     Medline TA:  RNA     Country:  United States    
Other Details:
Languages:  eng     Pagination:  936-44     Citation Subset:  IM    
Department of Biochemistry, Uniformed Services University of the Health Sciences (USUHS), Bethesda, Maryland 20814-4799, USA.
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MeSH Terms
Multiprotein Complexes / metabolism*
Protein Interaction Domains and Motifs
RNA / metabolism*
RNA Cap-Binding Proteins / chemistry*,  metabolism*
RNA-Binding Proteins / chemistry,  metabolism*
Saccharomyces cerevisiae / metabolism
Saccharomyces cerevisiae Proteins / chemistry*,  metabolism*
Grant Support
Reg. No./Substance:
0/LSM1 protein, S cerevisiae; 0/LSM7 protein, S cerevisiae; 0/Multiprotein Complexes; 0/PAT1 protein, S cerevisiae; 0/RNA Cap-Binding Proteins; 0/RNA-Binding Proteins; 0/Saccharomyces cerevisiae Proteins; 63231-63-0/RNA

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