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LSM8 Lsm8p

Lsm8p, Lsm8
This gene encodes a member of the like-Sm family of proteins. The encoded protein consists of a closed barrel shape, made up of five anti-parallel beta strands and an alpha helix. This protein partners with six paralogs to form a heteroheptameric ring which transiently binds U6 small nuclear RNAs and is involved in the general maturation of RNA in the nucleus. [provided by RefSeq, Jan 2010] (from NCBI)
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Top mentioned proteins: Lsm1, Lsm3p, caspase-3, POLYMERASE, Lsm6
Papers on Lsm8p
Arabidopsis thaliana LSM proteins function in mRNA splicing and degradation.
Kufel et al., Warsaw, Poland. In Nucleic Acids Res, 2013
In lsm8 and sad1/lsm5 mutants, U6 small nuclear RNA (snRNA) was reduced and unspliced mRNA precursors accumulated, whereas mRNA stability was mainly affected in plants lacking AtLSM1 and AtLSM5.
Analysis of Lsm1p and Lsm8p domains in the cellular localization of Lsm complexes in budding yeast.
Beggs et al., Edinburgh, United Kingdom. In Febs J, 2009
Results describe a range of mutant and hybrid Lsm1 and Lsm8 proteins, shedding light on the relative importance of their various domains in determining their localization and ability to support growth.
Requirements for nuclear localization of the Lsm2-8p complex and competition between nuclear and cytoplasmic Lsm complexes.
Beggs et al., Edinburgh, United Kingdom. In J Cell Sci, 2008
We show that, in yeast, the nuclear accumulation of Lsm proteins depends on complex formation and that the Lsm8p subunit plays a crucial role.
Hypoxia-regulated components of the U4/U6.U5 tri-small nuclear riboprotein complex: possible role in autosomal dominant retinitis pigmentosa.
Preising et al., Boca Raton, United States. In Mol Vis, 2007
Three IHR genes linked the U4/U6.U5 tri-snRNP complex to regulation by oxygenation: PRPF4; SART1, also known as 110 kDa SR-related protein of the U4/U6.U5 tri-snRNP or as hypoxia associated factor (HAF); and LSM8, U6 snRNA-associated Sm-like protein.
Nuclear pre-mRNA decapping and 5' degradation in yeast require the Lsm2-8p complex.
Tollervey et al., Edinburgh, United Kingdom. In Mol Cell Biol, 2004
Lsm2-8p complex normally targets nuclear RNA substrates for decapping
Identification and functional characterization of lsm proteins in Trypanosoma brucei.
Michaeli et al., Ramat Gan, Israel. In J Biol Chem, 2004
In this study, we identified seven Lsm proteins (Lsm2p to Lsm8p) and examined the function of Lsm3p and Lsm8p by RNA interference silencing.
A complex pathway for 3' processing of the yeast U3 snoRNA.
Tollervey et al., Edinburgh, United Kingdom. In Nucleic Acids Res, 2004
On depletion of any of the five essential proteins, Lsm2-5p or Lsm8p, the normal 3'-extended precursors to the U3 snoRNA were lost.
Lsm Proteins are required for normal processing and stability of ribosomal RNAs.
Tollervey et al., Edinburgh, United Kingdom. In J Biol Chem, 2003
Depletion of any of the essential Lsm proteins, Lsm2-5p or Lsm8p, delayed pre-rRNA processing and led to the accumulation of many aberrant processing intermediates, indicating that an Lsm complex is required to maintain the normally strict order of processing events.
Lsm proteins are required for normal processing of pre-tRNAs and their efficient association with La-homologous protein Lhp1p.
Tollervey et al., Edinburgh, United Kingdom. In Mol Cell Biol, 2002
Depletion of any of the five essential proteins Lsm2p to Lsm5p and Lsm8p leads to strong accumulation of all tested unspliced pre-tRNA species, as well as accumulation of 5' and 3' unprocessed species.
Multiple functional interactions between components of the Lsm2-Lsm8 complex, U6 snRNA, and the yeast La protein.
Wolin et al., New Haven, United States. In Genetics, 2001
Overexpression of LSM2 in the lsm8 mutant strain increases the levels of both Lsm8p and U6 snRNPs.
A Sm-like protein complex that participates in mRNA degradation.
Séraphin et al., Heidelberg, Germany. In Embo J, 2000
In eukaryotes, seven Sm proteins bind to the U1, U2, U4 and U5 spliceosomal snRNAs while seven Smlike proteins (Lsm2p-Lsm8p) are associated with U6 snRNA.
A role for the yeast La protein in U6 snRNP assembly: evidence that the La protein is a molecular chaperone for RNA polymerase III transcripts.
Wolin et al., New Haven, United States. In Embo J, 1999
This protein, Lsm8p, is a member of a family of proteins, known as Sm-like proteins, that shares two conserved motifs with the core Sm proteins of the U1, U2, U4 and U5 snRNPs.
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