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U6 snRNA-associated Sm-like protein LSm4

 
Known abbreviations: LSM4, SDB23, USS1, YER112W

 

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. LSM4 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. LSM4, 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. LSM4 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 LSm4 is involved: Pathways in which U6 snRNA-associated Sm-like protein LSm4 is involved:

NCBI GI number(s): 6320958
296144129
Species: Saccharomyces cerevisiae

Links to other databases:

Database ID Link
Uniprot P40070 P40070
BRENDA - -
KEGG sce:YER112W sce:YER112W
PFAM: PF01423
PF01423
InterPro: IPR010920
IPR001163
IPR006649
IPR010920
IPR001163
IPR006649
CATH: - -
SCOP: - -


Protein sequence:
MLPLYLLTNAKGQQMQIELKNGEIIQGILTNVDNWMNLTLSNVTEYSEES
AINSEDNAESSKAVKLNEIYIRGTFIKFIKLQDNIIDKVKQQINSNNNSN
SNGPGHKRYYNNRDSNNNRGNYNRRNNNNGNSNRRPYSQNRQYNNSNSSN
INNSINSINSNNQNMNNGLGGSVQHHFNSSSPQKVEF

U6 snRNA-associated Sm-like protein LSm4 (Saccharomyces cerevisiae) is product of expression of LSM4 gene.

References:

Title Authors Journal Publication date (Issue) PubMed ID
Global analysis of protein localization in budding yeast. Huh WK, Falvo JV, Gerke LC, Carroll AS, Howson RW, Weissman JS, O'Shea EK Nature 2003-10-16 (425) 14562095
The nucleotide sequence of Saccharomyces cerevisiae chromosome V. Dietrich FS, Mulligan J, Hennessy K, Yelton MA, Allen E, Araujo R, Aviles E, Berno A, Brennan T, Carpenter J, Chen E, Cherry JM, Chung E, Duncan M, Guzman E, Hartzell G, Hunicke-Smith S, Hyman RW, Kayser A, Komp C, Lashkari D, Lew H, Lin D, Mosedale D, Davis RW, et al. Nature 1997-05-01 (387) 9169868
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
A multidimensional chromatography technology for in-depth phosphoproteome analysis. Albuquerque CP, Smolka MB, Payne SH, Bafna V, Eng J, Zhou H Mol Cell Proteomics 2008-07-01 (7) 18407956
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
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
Yeast Sm-like proteins function in mRNA decapping and decay. Tharun S, He W, Mayes AE, Lennertz P, Beggs JD, Parker R Nature 2000-03-01 (404) 10761922
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
Identification and characterization of Uss1p (Sdb23p): a novel U6 snRNA-associated protein with significant similarity to core proteins of small nuclear ribonucleoproteins. Cooper M, Johnston LH, Beggs JD EMBO J 1995-05-01 (14) 7744012
Multiple SWI6-dependent cis-acting elements control SWI4 transcription through the cell cycle. Foster R, Mikesell GE, Breeden L Mol Cell Biol 1993-06-01 (13) 8497280



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

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