The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

LSM1  -  Lsm1p

Saccharomyces cerevisiae S288c

Synonyms: J0714, SPB8, SPB8 protein, Sm-like protein LSm1, YJL124C
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of LSM1

  • Previously, we used the ability of the higher eukaryotic positive-strand RNA virus brome mosaic virus (BMV) to replicate in yeast to show that the yeast LSM1 gene is required for recruiting BMV RNA from translation to replication [1].
  • Yeast Lsm1p-7p/Pat1p deadenylation-dependent mRNA-decapping factors are required for brome mosaic virus genomic RNA translation [1].

High impact information on LSM1

  • Here we show that mutations in seven yeast Lsm proteins (Lsm1-Lsm7) also lead to inhibition of mRNA decapping [2].
  • These results define an important rearrangement in mRNP organization and suggest that deadenylation promotes mRNA decapping by both the loss of Pab1p and the recruitment of the Lsm1p-7p complex [3].
  • Deletions of LSM1, 6, 7 and PAT1 genes increased the half-life of reporter mRNAs [4].
  • Surprisingly, using the tandem affinity purification (TAP) method, we identified Lsm1p among the subunits associated with Lsm3p [4].
  • Using the ability of BMV to replicate in yeast, we show that efficient BMV RNA replication requires Lsm1p, a yeast protein related to core RNA splicing factors but shown herein to be cytoplasmic [5].

Biological context of LSM1


Anatomical context of LSM1

  • High-resolution sucrose density gradient analysis showed that, while mutating factors in the Lsm1p-7p/Pat1p complex completely inhibited viral RNA translation, the levels of viral RNA associated with ribosomes were only slightly reduced in mutant yeast [1].

Other interactions of LSM1

  • First, mutations in the LSM1 to LSM7, as well as PAT1, genes led to the accumulation of MFA2pG and PGK1pG transcripts that had been shortened by 10-20 nucleotides at their 3' ends (referred to as trimming) [9].
  • Interestingly, the temperature-sensitive allele of eIF4E does not suppress the decapping defect seen in strains lacking the decapping activators, Lsm1p and Pat1p [10].
  • Here we report that mature heat shock and MET mRNAs that are trapped in the nucleus due to a block in mRNA export were strongly stabilized in strains lacking Lsm6p or the nucleus-specific Lsm8p protein but not by the absence of the cytoplasmic Lsm1p [11].
  • The role of Dhh1p in decapping appears to be direct, as Dhh1p physically interacts with several proteins involved in mRNA decapping including the decapping enzyme Dcp1p, as well as Lsm1p and Pat1p/Mrt1p, which function to enhance the decapping rate [12].
  • Lsm1p is the unique member of the Lsm1p-7p complex, distinguishing that complex from the functionally different Lsm2p-8p complex [6].


  1. Yeast Lsm1p-7p/Pat1p deadenylation-dependent mRNA-decapping factors are required for brome mosaic virus genomic RNA translation. Noueiry, A.O., Diez, J., Falk, S.P., Chen, J., Ahlquist, P. Mol. Cell. Biol. (2003) [Pubmed]
  2. Yeast Sm-like proteins function in mRNA decapping and decay. Tharun, S., He, W., Mayes, A.E., Lennertz, P., Beggs, J.D., Parker, R. Nature (2000) [Pubmed]
  3. Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs. Tharun, S., Parker, R. Mol. Cell (2001) [Pubmed]
  4. A Sm-like protein complex that participates in mRNA degradation. Bouveret, E., Rigaut, G., Shevchenko, A., Wilm, M., Séraphin, B. EMBO J. (2000) [Pubmed]
  5. Identification and characterization of a host protein required for efficient template selection in viral RNA replication. Díez, J., Ishikawa, M., Kaido, M., Ahlquist, P. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  6. Mutations in the Saccharomyces cerevisiae LSM1 gene that affect mRNA decapping and 3' end protection. Tharun, S., Muhlrad, D., Chowdhury, A., Parker, R. Genetics (2005) [Pubmed]
  7. Capped mRNA degradation intermediates accumulate in the yeast spb8-2 mutant. Boeck, R., Lapeyre, B., Brown, C.E., Sachs, A.B. Mol. Cell. Biol. (1998) [Pubmed]
  8. CaSm-mediated cellular transformation is associated with altered gene expression and messenger RNA stability. Fraser, M.M., Watson, P.M., Fraig, M.M., Kelley, J.R., Nelson, P.S., Boylan, A.M., Cole, D.J., Watson, D.K. Cancer Res. (2005) [Pubmed]
  9. The yeast cytoplasmic LsmI/Pat1p complex protects mRNA 3' termini from partial degradation. He, W., Parker, R. Genetics (2001) [Pubmed]
  10. mRNA decapping in yeast requires dissociation of the cap binding protein, eukaryotic translation initiation factor 4E. Schwartz, D.C., Parker, R. Mol. Cell. Biol. (2000) [Pubmed]
  11. Nuclear pre-mRNA decapping and 5' degradation in yeast require the Lsm2-8p complex. Kufel, J., Bousquet-Antonelli, C., Beggs, J.D., Tollervey, D. Mol. Cell. Biol. (2004) [Pubmed]
  12. The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes. Coller, J.M., Tucker, M., Sheth, U., Valencia-Sanchez, M.A., Parker, R. RNA (2001) [Pubmed]
WikiGenes - Universities