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Exosome complex component RRP42

 
Known also as: Ribosomal RNA-processing protein 42

Known abbreviations: Rrp42, YDL111C


FUNCTION:

  • exosome component without exonuclease activity (PMID: 17942686),
  • required for degradation of 3'-end of the 7S pre-RNA to generate mature 5.8S (S) rRNA and 5.8S(L) rRNA (cleavage at site C2 in 3'-5' direction) (PMID:9390555, 10508172, 9891085, 9463390),
  • Required for degradation of 5' end of the 35S pre-rRNA in 3'-5' direction (cleavage at site A0) (PMID: 9463390, 10465791).

CELLULAR LOCALIZATION:

  • cytoplasmic exosome (RNase complex) (PMID: 10465791)
  • nuclear exosome (RNase complex) (PMID: 10465791)

DOMAIN ARCHITECTURE:

protein lenght: 265 aa (UniProt)
PH_domain1: 30 - 155(InterPro)
PH_domain2: 183 - 254

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.



This protein can be a part of a given complexes:
NCBI GI number(s): 1431160
Species: Saccharomyces cerevisiae

Links to other databases:

Database ID Link
Uniprot Q12277 Q12277
BRENDA - -
KEGG sce:YDL111C sce:YDL111C
PFAM: PF01138
PF01138
InterPro: IPR001247
IPR020568
IPR001247
IPR020568
CATH: - -
SCOP: - -


Protein sequence:
MSLSVAEKSYLYDSLASTPSIRPDGRLPHQFRPIEIFTDFLPSSNGSSRI
IASDGSECIVSIKSKVVDHHVENELLQVDVDIAGQRDDALVVETITSLLN
KVLKSGSGVDSSKLQLTKKYSFKIFVDVLVISSHSHPVSLISFAIYSALN
STYLPKLISAFDDLEVEELPTFHDYDMVKLDINPPLVFILAVVGNNMLLD
PAANESEVANNGLIISWSNGKITSPIRSVALNDSNVKSFKPHLLKQGLAM
VEKYAPDVVRSLENL

Exosome complex component RRP42 (Saccharomyces cerevisiae) is product of expression of RRP42 gene.

Exosome complex component RRP42 (Saccharomyces cerevisiae) belongs to following protein families:
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 exosome: a conserved eukaryotic RNA processing complex containing multiple 3'-->5' exoribonucleases. Mitchell P, Petfalski E, Shevchenko A, Mann M, Tollervey D Cell 1997-11-14 (91) 9390555
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 3' to 5' degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3' to 5' exonucleases of the exosome complex. Anderson JS, Parker RP EMBO J 1998-03-02 (17) 9482746
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
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
The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open reading frames. Boskovic J, Soler-Mira A, Garcia-Cantalejo JM, Ballesta JP, Jimenez A, Remacha M Yeast 1996-10-01 (12) 8923743



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Entry added on: 2011-01-22 14:12:45, by a user: kasia

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