Genomes and Genes
Gene Symbol: LSM7
Description: Sm-like protein LSM7
Alias: Sm-like protein LSM7
Species: Saccharomyces cerevisiae S288c
- Mayes A, Verdone L, Legrain P, Beggs J. Characterization of Sm-like proteins in yeast and their association with U6 snRNA. EMBO J. 1999;18:4321-31 pubmed..We discuss the possible existence and functions of alternative Lsm complexes, including the likelihood that they are involved in processes other than pre-mRNA splicing. ..
- Karaduman R, Dube P, Stark H, Fabrizio P, Kastner B, Luhrmann R. Structure of yeast U6 snRNPs: arrangement of Prp24p and the LSm complex as revealed by electron microscopy. RNA. 2008;14:2528-37 pubmed publisher..Further, LSmp-Prp24p interactions may be restricted to the closed form, which appears to represent the solution structure of the U6 snRNP particle. ..
- Luhtala N, Parker R. LSM1 over-expression in Saccharomyces cerevisiae depletes U6 snRNA levels. Nucleic Acids Res. 2009;37:5529-36 pubmed publisher..These results suggest that inhibition of splicing and/or deadenylation may be effective therapies for Lsm1-over-expressing tumors. ..
- Sobti M, Cubeddu L, Haynes P, Mabbutt B. Engineered rings of mixed yeast Lsm proteins show differential interactions with translation factors and U-rich RNA. Biochemistry. 2010;49:2335-45 pubmed publisher..Our findings suggest Lsm1 and/or Lsm4 can interact with translationally active mRNA. ..
- Chowdhury A, Tharun S. lsm1 mutations impairing the ability of the Lsm1p-7p-Pat1p complex to preferentially bind to oligoadenylated RNA affect mRNA decay in vivo. RNA. 2008;14:2149-58 pubmed publisher..These results underscore the importance of Lsm1p-7p-Pat1p complex-mRNA interaction for mRNA decay in vivo and imply that the oligo(A) tail mediated enhancement of such interaction is crucial in that process. ..
- Karaduman R, Fabrizio P, Hartmuth K, Urlaub H, Luhrmann R. RNA structure and RNA-protein interactions in purified yeast U6 snRNPs. J Mol Biol. 2006;356:1248-62 pubmed..Interestingly, we find that the open structure of the yeast U6 snRNA in native snRNPs can also be adopted by human U6 and U6atac snRNAs. ..
- Didychuk A, Montemayor E, Carrocci T, DeLaitsch A, Lucarelli S, Westler W, et al. Usb1 controls U6 snRNP assembly through evolutionarily divergent cyclic phosphodiesterase activities. Nat Commun. 2017;8:497 pubmed publisher..Here the authors characterize the enzymatic activities and structures of yeast and human U6 RNA processing enzyme Usb1, reconstitute post-transcriptional assembly of yeast U6 snRNP in vitro, and propose a model for U6 snRNP assembly. ..
- Sharif H, Conti E. Architecture of the Lsm1-7-Pat1 complex: a conserved assembly in eukaryotic mRNA turnover. Cell Rep. 2013;5:283-91 pubmed publisher..These results show how the auxiliary domains and the canonical Sm folds of the Lsm1-7 complex are organized in order to mediate and modulate macromolecular interactions. ..
- Chowdhury A, Raju K, Kalurupalle S, Tharun S. Both Sm-domain and C-terminal extension of Lsm1 are important for the RNA-binding activity of the Lsm1-7-Pat1 complex. RNA. 2012;18:936-44 pubmed publisher..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' ..
- Wu D, Muhlrad D, Bowler M, Jiang S, Liu Z, Parker R, et al. Lsm2 and Lsm3 bridge the interaction of the Lsm1-7 complex with Pat1 for decapping activation. Cell Res. 2014;24:233-46 pubmed publisher..Based on the structure of Lsm2-3-Pat1C, a model of Lsm1-7-Pat1 complex is constructed and how RNA binds to this complex is discussed. ..
- Fang N, Chan G, Zhu M, Comyn S, Persaud A, Deshaies R, et al. Rsp5/Nedd4 is the main ubiquitin ligase that targets cytosolic misfolded proteins following heat stress. Nat Cell Biol. 2014;16:1227-37 pubmed publisher..Our results support a bipartite recognition mechanism combining direct and chaperone-dependent ubiquitylation of misfolded cytosolic proteins by Rsp5. ..
- Tharun S. Purification and analysis of the decapping activator Lsm1p-7p-Pat1p complex from yeast. Methods Enzymol. 2008;448:41-55 pubmed publisher..2007). These observations, therefore, highlighted the importance of the intrinsic RNA binding properties of this complex as key determinants of its in vivo functions. ..
- Fang N, Ng A, Measday V, Mayor T. Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins. Nat Cell Biol. 2011;13:1344-52 pubmed publisher..These findings indicate that Hul5 is involved in a cytosolic protein quality control pathway that targets misfolded proteins for degradation. ..
- Chowdhury A, Kalurupalle S, Tharun S. Pat1 contributes to the RNA binding activity of the Lsm1-7-Pat1 complex. RNA. 2014;20:1465-75 pubmed publisher..This complex is made up of the seven Sm-like proteins, Lsm1 through Lsm7, and the Pat1 protein...