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U6 snRNA-associated Sm-like protein LSm2

 
Known also as: Small nuclear ribonucleoprotein D homolog SNP3

Known abbreviations: LSM2, SMX5, SNP3, YBL026W, YBL0425

 

FUNCTION:
 
Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Component of the cytoplasmic LSM1-LSM7 complex which is thought to be involved in mRNA degradation by activating the decapping step. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 snRNP, U4/U6.U5 snRNP, and free U6 snRNP). It binds directly to the U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. It probably also is involved degradation of nuclear pre-mRNA by targeting them for decapping. LSM2 binds specifically to the 3'-terminal U-tract of U6 snRNA. LSM2-LSM8 probably is involved in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. LSM2, probably in a complex that contains LSM2-LSM7 but not LSM1 or LSM8, associates with the precursor of the RNA component of RNase P (pre-P RNA) and may be involved in maturing pre-P RNA. LSM2 is required for processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. 
 
SUBUNIT STRUCTURE:
 
Component of the heptameric LSM1-LSM7 complex, which consists of LSM1, LSM2, LSM3, LSM4, LSM5, LSM6 and LSM7. Component of the heptameric LSM2-LSM8 complex, which consists of LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. LSM2-LSM8 associates with PAT1 and XRN1. The LSm subunits form a seven-membered ring structure with a doughnut shape (By similarity). A complex comprising LSM2-LSM7 without LSM1 or LSM8 may exist.
 
CELLULAR LOCALIZATION:
 
Nucleus. Cytoplasm.



This protein can be a part of a given complexes: Activities in which U6 snRNA-associated Sm-like protein LSm2 is involved: Pathways in which U6 snRNA-associated Sm-like protein LSm2 is involved:

NCBI GI number(s): 6319445
Species: Saccharomyces cerevisiae

Links to other databases:

Database ID Link
Uniprot P38203 P38203
BRENDA - -
KEGG sce:YBL026W sce:YBL026W
PFAM: PF01423
PF01423
InterPro: IPR010920
IPR001163
IPR006649
IPR016654
IPR010920
IPR001163
IPR006649
IPR016654
CATH: - -
SCOP: - -


Protein sequence:
MLFFSFFKTLVDQEVVVELKNDIEIKGTLQSVDQFLNLKLDNISCTDEKK
YPHLGSVRNIFIRGSTVRYVYLNKNMVDTNLLQDATRREVMTERK

U6 snRNA-associated Sm-like protein LSm2 (Saccharomyces cerevisiae) is product of expression of LSM2 gene.

References:

Title Authors Journal Publication date (Issue) PubMed ID
Complete DNA sequence of yeast chromosome II. Feldmann H, Aigle M, Aljinovic G, Andre B, Baclet MC, Barthe C, Baur A, Becam AM, Biteau N, Boles E, Brandt T, Brendel M, Bruckner M, Bussereau F, Christiansen C, Contreras R, Crouzet M, Cziepluch C, Demolis N, Delaveau T, Doignon F, Domdey H, Dusterhus S, Dubois E, Dujon B, El Bakkoury M, Entian KD EMBO J 1994-12-15 (13) 7813418
Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin. Salgado-Garrido J, Bragado-Nilsson E, Kandels-Lewis S, Seraphin B EMBO J 1999-06-15 (18) 10369684
Global analysis of protein expression in yeast. Ghaemmaghami S, Huh WK, Bower K, Howson RW, Belle A, Dephoure N, O'Shea EK, Weissman JS Nature 2003-10-16 (425) 14562106
Characterization of Sm-like proteins in yeast and their association with U6 snRNA. Mayes AE, Verdone L, Legrain P, Beggs JD EMBO J 1999-08-02 (18) 10428970
Identification by mass spectrometry and functional analysis of novel proteins of the yeast [U4/U6.U5] tri-snRNP. Gottschalk A, Neubauer G, Banroques J, Mann M, Luhrmann R, Fabrizio P EMBO J 1999-08-16 (18) 10449419
A Sm-like protein complex that participates in mRNA degradation. Bouveret E, Rigaut G, Shevchenko A, Wilm M, Seraphin B EMBO J 2000-04-03 (19) 10747033
Nuclear pre-mRNA decapping and 5' degradation in yeast require the Lsm2-8p complex. Kufel J, Bousquet-Antonelli C, Beggs JD, Tollervey D Mol Cell Biol 2004-11-01 (24) 15485930
Lsm proteins are required for normal processing of pre-tRNAs and their efficient association with La-homologous protein Lhp1p. Kufel J, Allmang C, Verdone L, Beggs JD, Tollervey D Mol Cell Biol 2002-07-01 (22) 12077351
Lsm Proteins are required for normal processing and stability of ribosomal RNAs. Kufel J, Allmang C, Petfalski E, Beggs J, Tollervey D J Biol Chem 2003-02-24 (278) 12438310
Analysis of a 17.4 kb DNA segment of yeast chromosome II encompassing the ribosomal protein L19 as well as proteins with homologies to components of the hnRNP and snRNP complexes and to the human proliferation-associated p120 antigen. Van Dyck L, Jonniaux JL, de Melo Barreiros T, Kleine K, Goffeau A Yeast 1994-12-01 (10) 7725803
A complex pathway for 3' processing of the yeast U3 snoRNA. Kufel J, Allmang C, Verdone L, Beggs J, Tollervey D Nucleic Acids Res 2003-12-01 (31) 14627812



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Last modification of this entry: Sept. 25, 2012.

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