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Exosome complex component CSL4

 
Known also as: CEP1 synthetic lethal protein 4

Known abbreviations: CSL4, SKI4, YNL232W, N1154

FUNCTION:
  • exosome component without catalytic activity  (PMID: 17942686)
  • RNA-binding protein (PMID: 17942686)
  • degradation of deadenylated mRNA in 3'-5' direction  (PMID: 12364597) zinc-ribbon domain is required for exosome-mediated mRNA decay (PMID: 19060898)
CELLULAR LOCALIZATION:
 
CytoplasmNucleus › nucleolus
 
DOMAIN ARCHITECTURE:
  • zinc-ribbon domain
  • S1 domain
  • RPL27-like domain (PMID: 19060898)
?SUBUNIT STRUCTURE:
 
Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which associates with catalytic subunits DIS3 and RRP6 in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits and peripheral S1 domain-containing components CSL4, RRP4 and RRP40 located on the top of the ring structure.
 
OTHER:
 
Includes regions homologous to the S1 RNA-binding domain from E.coli (PMID: 10465791) and KH domain (PMID: 17159918)



This protein can be a part of a given complexes:
NCBI GI number(s): 6324097
296147546
Species: Saccharomyces cerevisiae

Links to other databases:

Database ID Link
Uniprot P53859 P53859
BRENDA - -
KEGG sce:YNL232W sce:YNL232W
PFAM: PF10447
PF10447
InterPro: IPR019495
IPR019495
CATH: - -
SCOP: - -


Protein sequence:
MACNFQFPEIAYPGKLICPQYGTENKDGEDIIFNYVPGPGTKLIQYEHNG
RTLEAITATLVGTVRCEEEKKTDQEEEREGTDQSTEEEKSVDASPNDVTR
RTVKNILVSVLPGTEKGRKTNKYANNDFANNLPKEGDIVLTRVTRLSLQR
ANVEILAVEDKPSPIDSGIGSNGSGIVAAGGGSGAATFSVSQASSDLGET
FRGIIRSQDVRSTDRDRVKVIECFKPGDIVRAQVLSLGDGTNYYLTTARN
DLGVVFARAANGAGGLMYATDWQMMTSPVTGATEKRKCAKPF

Exosome complex component CSL4 (Saccharomyces cerevisiae) is product of expression of CSL4 gene.

References:

Title Authors Journal Publication date (Issue) PubMed ID
Reconstitution, activities, and structure of the eukaryotic RNA exosome. Liu Q, Greimann JC, Lima CD Cell 2006-12-15 (127) 17174896
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 yeast exosome and human PM-Scl are related complexes of 3' --> 5' exonucleases. Allmang C, Petfalski E, Podtelejnikov A, Mann M, Tollervey D, Mitchell P Genes Dev 1999-08-15 (13) 10465791
The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities. Schaeffer D, Tsanova B, Barbas A, Reis FP, Dastidar EG, Sanchez-Rotunno M, Arraiano CM, van Hoof A Nat Struct Mol Biol 2009-02-01 (16) 19060898
The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications. Philippsen P, Kleine K, Pohlmann R, Dusterhoft A, Hamberg K, Hegemann JH, Obermaier B, Urrestarazu LA, Aert R, Albermann K Nature 1997-05-01 (387) 9169873
A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Dziembowski A, Lorentzen E, Conti E, Seraphin B Nat Struct Mol Biol 2007-02-01 (14) 17173052
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
Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry. Chi A, Huttenhower C, Geer LY, Coon JJ, Syka JE, Bai DL, Shabanowitz J, Burke DJ, Troyanskaya OG, Hunt DF Proc Natl Acad Sci U S A 2007-01-13 (104) 17287358
The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open reading frames including a novel gene encoding a globin-like domain. Pandolfo D, De Antoni A, Lanfranchi G, Valle G Yeast 1996-09-01 (12) 8896273
Mutations synthetically lethal with cep1 target S. cerevisiae kinetochore components. Baker RE, Harris K, Zhang K Genetics 1998-05-01 (149) 9584087



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

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