Welcome! Click here to login or here to register.
Home
Pathways
Proteins
Catalytic RNA molecules
Enzymatic complexes
Structures
Publications
Draw a picture
 
Search
 
Links
Help
Contact





Bujnicki Lab Homepage

U6 snRNA-associated Sm-like protein LSm6

 
Known abbreviations: LSM6, YDR378C, D9481.18

 

FUNCTION:
 
Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner, facilitating the efficient association of RNA processing factors with their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is thought to be involved in mRNA degradation by activating the decapping step in the 5'-to-3' mRNA decay pathway. In association with PAT1, LSM1-LSM7 binds directly to RNAs near the 3'-end and prefers oligoadenylated RNAs over polyadenylated RNAs. 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 di-snRNP, U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds directly to the 3'-terminal U-tract of U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. LSM2-LSM8 probably also is involved degradation of nuclear pre-mRNA by targeting them for decapping, and in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. Component of a nucleolar LSM2-LSM7 complex, which associates with the precursor of the RNA component of RNase P (pre-P RNA) and with the small nucleolar RNA (snoRNA) snR5. It may play a role in the maturation of a subset of nucleolus-associated small RNAs. 
 
SUBUNIT STRUCTURE:
 
Component of the heptameric LSM1-LSM7 complex, which consists of LSM1, LSM2, LSM3, LSM4, LSM5, LSM6 and LSM7. LSM1-LSM7 associates with PAT1 and XRN1. Component of the heptameric LSM2-LSM8 complex, which consists of LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. The LSm subunits form a seven-membered ring structure with a doughnut shape By similarity. Component of a LSM2-LSM7 complex, which consists of at least LSM2, LSM3, LSM4, LSM5, LSM6 and LSM7. It is not known whether another protein replaces the missing LSm to form a novel heptameric complex.
 
CELLULAR LOCALIZATION:
 
Cytoplasm. Nucleus › nucleolus. Note: LSM1 and LSM8 act competitively with respect to the localization of LSM1-LSM7 to the cytoplasm and LSM2-LSM8 to the nucleus. LSm proteins shift to the cytoplasm under conditions of stress. 



This protein can be a part of a given complexes: Activities in which U6 snRNA-associated Sm-like protein LSm6 is involved: Pathways in which U6 snRNA-associated Sm-like protein LSm6 is involved:

NCBI GI number(s): 82795247
296143728
Species: Saccharomyces cerevisiae

Links to other databases:

Database ID Link
Uniprot Q06406 Q06406
BRENDA - -
KEGG sce:YDR378C sce:YDR378C
PFAM: PF01423
PF01423
InterPro: IPR010920
IPR001163
IPR006649
IPR010920
IPR001163
IPR006649
CATH: - -
SCOP: - -


Protein sequence:
MSGKASTEGSVTTEFLSDIIGKTVNVKLASGLLYSGRLESIDGFMNVALS
SATEHYESNNNKLLNKFNSDVFLRGTQVMYISEQKI

U6 snRNA-associated Sm-like protein LSm6 (Saccharomyces cerevisiae) is product of expression of LSM6 gene.

References:

Title Authors Journal Publication date (Issue) PubMed ID
The nucleotide sequence of Saccharomyces cerevisiae chromosome IV. Jacq C, Alt-Morbe J, Andre B, Arnold W, Bahr A, Ballesta JP, Bargues M, Baron L, Becker A, Biteau N, Blocker H, Blugeon C, Boskovic J, Brandt P, Bruckner M, Buitrago MJ, Coster F, Delaveau T, del Rey F, Dujon B, Eide LG, Garcia-Cantalejo JM, Goffeau A, Gomez-Peris A, Zaccaria P, et al. Nature 1997-05-01 (387) 9169867
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
An Lsm2-Lsm7 complex in Saccharomyces cerevisiae associates with the small nucleolar RNA snR5. Fernandez CF, Pannone BK, Chen X, Fuchs G, Wolin SL Mol Biol Cell 2004-06-01 (15) 15075370
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
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
Mapping of transcription start sites in Saccharomyces cerevisiae using 5' SAGE. Zhang Z, Dietrich FS Nucleic Acids Res 2005-01-01 (33) 15905473
Requirements for nuclear localization of the Lsm2-8p complex and competition between nuclear and cytoplasmic Lsm complexes. Spiller MP, Reijns MA, Beggs JD J Cell Sci 2007-12-15 (120) 18029398
The decapping activator Lsm1p-7p-Pat1p complex has the intrinsic ability to distinguish between oligoadenylated and polyadenylated RNAs. Chowdhury A, Mukhopadhyay J, Tharun S RNA 2007-07-01 (13) 17513695



Add your own comment!


There are no comments yet.

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

Welcome stranger! Click here to login or here to register.