LSM3

Summary

Gene Symbol: LSM3
Description: U4/U6-U5 snRNP complex subunit LSM3
Alias: SMX4, USS2, U4/U6-U5 snRNP complex subunit LSM3
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. 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. ..
  2. Häcker I, Sander B, Golas M, Wolf E, Karagöz E, Kastner B, et al. Localization of Prp8, Brr2, Snu114 and U4/U6 proteins in the yeast tri-snRNP by electron microscopy. Nat Struct Mol Biol. 2008;15:1206-12 pubmed publisher
    ..The head and arm adopt variable relative positions. This molecular organization and dynamics suggest possible scenarios for structural events during catalytic activation. ..
  3. Chowdhury A, Mukhopadhyay J, Tharun S. The decapping activator Lsm1p-7p-Pat1p complex has the intrinsic ability to distinguish between oligoadenylated and polyadenylated RNAs. RNA. 2007;13:998-1016 pubmed
    ..These results indicate that the intrinsic RNA-binding characteristics of this complex form a critical determinant of its in vivo interactions and functions. ..
  4. Salgado Garrido J, Bragado Nilsson E, Kandels Lewis S, Seraphin B. Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin. EMBO J. 1999;18:3451-62 pubmed
    ..We also identified archaeal proteins related to Sm and Sm-like proteins. Our results demonstrate that Sm and Sm-like proteins assemble in at least two functionally conserved complexes of deep evolutionary origin. ..
  5. Bouveret E, Rigaut G, Shevchenko A, Wilm M, Seraphin B. A Sm-like protein complex that participates in mRNA degradation. EMBO J. 2000;19:1661-71 pubmed
    ..These results indicate the involvement of a new conserved Sm-like protein complex and a new factor, Pat1p, in mRNA degradation and suggest a physical connection between decapping and exonuclease trimming. ..
  6. Naidoo N, Harrop S, Sobti M, Haynes P, Szymczyna B, Williamson J, et al. Crystal structure of Lsm3 octamer from Saccharomyces cerevisiae: implications for Lsm ring organisation and recruitment. J Mol Biol. 2008;377:1357-71 pubmed publisher
    ..The crystal structure of yeast Lsm3 reveals a new organisation of the L/Sm beta-propeller ring, containing eight protein subunits...
  7. Tharun S, He W, Mayes A, Lennertz P, Beggs J, Parker R. Yeast Sm-like proteins function in mRNA decapping and decay. Nature. 2000;404:515-8 pubmed
    ..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. ..
  8. Pannone B, Kim S, Noe D, Wolin S. Multiple functional interactions between components of the Lsm2-Lsm8 complex, U6 snRNA, and the yeast La protein. Genetics. 2001;158:187-96 pubmed
    ..Our experiments are consistent with a model in which Lsm2p and Lsm4p contact Lsm8p in the Lsm2-Lsm8 ring and suggest that Lhp1p acts redundantly with the entire Lsm2-Lsm8 complex to stabilize nascent U6 snRNA. ..
  9. 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. ..

More Information

Publications24

  1. 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. ..
  2. 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. ..
  3. 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
    ..Thus, unlike most Sm-like proteins, Lsm1 uniquely requires both its Sm-domain and CTD for its normal RNA-binding function. ..
  4. 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
    ..Pat1 reveals that Pat1 recognition is not mediated by the distinguishing cytoplasmic subunit, Lsm1, but by Lsm2 and Lsm3. These results show how the auxiliary domains and the canonical Sm folds of the Lsm1-7 complex are organized in ..
  5. Camasses A, Bragado Nilsson E, Martin R, Seraphin B, Bordonne R. Interactions within the yeast Sm core complex: from proteins to amino acids. Mol Cell Biol. 1998;18:1956-66 pubmed
    ..Surprisingly, we observed that other evolutionarily conserved positions are tolerant to mutations, with substitutions affecting binding to SmF and SmG only mildly and conferring a wild-type growth phenotype. ..
  6. Fernandez C, Pannone B, Chen X, Fuchs G, Wolin S. An Lsm2-Lsm7 complex in Saccharomyces cerevisiae associates with the small nucleolar RNA snR5. Mol Biol Cell. 2004;15:2842-52 pubmed
  7. Taoka M, Yamauchi Y, Nobe Y, Masaki S, Nakayama H, Ishikawa H, et al. An analytical platform for mass spectrometry-based identification and chemical analysis of RNA in ribonucleoprotein complexes. Nucleic Acids Res. 2009;37:e140 pubmed publisher
  8. Vidal V, Verdone L, Mayes A, Beggs J. Characterization of U6 snRNA-protein interactions. RNA. 1999;5:1470-81 pubmed
    ..Interestingly, the Lsm proteins associate efficiently with the 3' half of U6, which contains the 3' stem-loop and uridine-rich 3' end, suggesting that the Lsm and Sm proteins may recognize similar features in RNAs. ..
  9. 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
    ..Here, we show that Lsm2 and Lsm3 bridge the interaction between the C-terminus of Pat1 (Pat1C) and the Lsm1-7 complex...
  10. 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. ..
  11. Kufel J, Allmang C, Petfalski E, Beggs J, Tollervey D. Lsm Proteins are required for normal processing and stability of ribosomal RNAs. J Biol Chem. 2003;278:2147-56 pubmed
    ..We propose that Lsm proteins facilitate RNA protein interactions and structural changes required during ribosomal subunit assembly. ..
  12. 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. ..
  13. 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. ..
  14. Collins B, Cubeddu L, Naidoo N, Harrop S, Kornfeld G, Dawes I, et al. Homomeric ring assemblies of eukaryotic Sm proteins have affinity for both RNA and DNA. Crystal structure of an oligomeric complex of yeast SmF. J Biol Chem. 2003;278:17291-8 pubmed
    ..Furthermore, we demonstrate that the homomeric assemblies of yeast Sm and Lsm proteins are capable of binding not only to oligo(U) RNA but, in the case of SmF, also to oligo(dT) single-stranded DNA. ..
  15. Spiller M, Reijns M, Beggs J. Requirements for nuclear localization of the Lsm2-8p complex and competition between nuclear and cytoplasmic Lsm complexes. J Cell Sci. 2007;120:4310-20 pubmed
    ..A shift of Lsm proteins from the nucleus to the cytoplasm under stress conditions indicates that this competition is biologically significant. ..