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Protein DOM34

 
Known abbreviations: DOM34, YNL001W, N2016

 

FUNCTION:
 
Involved in protein translation. Together with HBS1, may function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs. The complex formed by DOM34 and HBS1 has ribonuclease activity towards double-stranded RNA substrates, but does not cleave single-stranded RNA. Acts as endonuclease; has no exonuclease activity. Increases the affinity of HBS1 for GTP, but nor for GDP. Promotes G1 progression and differentiation and is involved in mitotic and meiotic cell divisions. 
 
COFACTOR:
 
Divalent metal cations.
 
SUBUNIT STRUCTURE:
 
Monomer. Interacts with HBS1.
 
CELLULAR LOCALIZATION:
 
Cytoplasm 
 
DOMAIN:
 
The N-terminal domain has the RNA-binding Sm fold. It may harbor the endoribonuclease activity.



Activities in which Protein DOM34 is involved: Pathways in which Protein DOM34 is involved:

NCBI GI number(s): 6324327
296147763
Species: Saccharomyces cerevisiae

Links to other databases:

Database ID Link
Uniprot P33309 P33309
BRENDA - -
KEGG sce:YNL001W sce:YNL001W
PFAM: PF03463
PF03464
PF03465
PF03463
PF03464
PF03465
InterPro: IPR005140
IPR005141
IPR005142
IPR004405
IPR005140
IPR005141
IPR005142
IPR004405
CATH: - -
SCOP: - -
Solved crystal structures: 2VGM
2VGN
3J16
3IZQ
[PDB] [details]
[PDB] [details]
[PDB] [details]
[PDB] [details]


Protein sequence:
MKVISLKKDSFNKGGAVITLLPEDKEDLFTVYQIVDKDDELIFKKKFTSK
LDEAGKKKSTDLVKLKIKVISEDFDMKDEYLKYKGVTVTDESGASNVDIP
VGKYLSFTLDYVYPFTIIKQNFNKFMQKLLNEACNIEYKSDTAAVVLQEG
IAHVCLVTSSSTILKQKIEYSMPKKKRTTDVLKFDEKTEKFYKAIYSAMK
KDLNFDKLKTIILCSPGFYAKILMDKIFQYAEEEHNKKILDNKGMFFIAH
CSTGYLQGINEVLKNPLYASKLQDTKYSKEIMVMDEFLLHLNKDDDKAWY
GEKEVVKAAEYGAISYLLLTDKVLHSDNIAQREEYLKLMDSVESNGGKAL
VLSTLHSLGEELDQLTGIACILKYPLPDLDEDDGEE

Protein DOM34 (Saccharomyces cerevisiae) is product of expression of DOM34 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
Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation. Doma MK, Parker R Nature 2006-03-23 (440) 16554824
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
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
Novel G-protein complex whose requirement is linked to the translational status of the cell. Carr-Schmid A, Pfund C, Craig EA, Kinzy TG Mol Cell Biol 2002-04-01 (22) 11909951
Two yeast chromosomes are related by a fossil duplication of their centromeric regions. Lalo D, Stettler S, Mariotte S, Slonimski PP, Thuriaux P C R Acad Sci III 1993-01-01 (316) 8402262
Organization of the centromeric region of chromosome XIV in Saccharomyces cerevisiae. Lalo D, Stettler S, Mariotte S, Gendreau E, Thuriaux P Yeast 1994-04-01 (10) 7941739
Nucleotide sequence analysis of an 8887 bp region of the left arm of yeast chromosome XIV, encompassing the centromere sequence. Verhasselt P, Aert R, Voet M, Volckaert G Yeast 1994-07-01 (10) 7985421
Structural and functional insights into Dom34, a key component of no-go mRNA decay. Lee HH, Kim YS, Kim KH, Heo I, Kim SK, Kim O, Kim HK, Yoon JY, Kim HS, Kim do J, Lee SJ, Yoon HJ, Kim SJ, Lee BG, Song HK, Kim VN, Park CM, Suh SW Mol Cell 2007-09-21 (27) 17889667
Structure of yeast Dom34: a protein related to translation termination factor Erf1 and involved in No-Go decay. Graille M, Chaillet M, van Tilbeurgh H J Biol Chem 2008-03-14 (283) 18180287



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

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