title: Structural and functional insights into Dom34, a key component of no-go mRNA decay.
abstract: The yeast protein Dom34 is a key component of no-go decay, by which mRNAs with translational stalls are endonucleolytically cleaved and subsequently degraded. However, the identity of the endoribonuclease is unknown. Homologs of Dom34, called Pelota, are broadly conserved in eukaryotes and archaea. To gain insights into the structure and function of Dom34/Pelota, we have determined the structure of Pelota from Thermoplasma acidophilum (Ta Pelota) and investigated the ribonuclease activity of Dom34/Pelota. The structure of Ta Pelota is tripartite, and its domain 1 has the RNA-binding Sm fold. We have discovered that Ta Pelota has a ribonuclease activity and that its domain 1 is sufficient for the catalytic activity. We also demonstrate that domain 1 of Dom34 has an endoribonuclease activity against defined RNA substrates containing a stem loop, which supports a direct catalytic role of yeast Dom34 in no-go mRNA decay.
authors: Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151-747, Korea.
authors: Hyung Ho
authors: HH
authors: Lee
authors: Youn-Sung
authors: YS
authors: Kim
authors: Kyoung Hoon
authors: KH
authors: Kim
authors: Inha
authors: I
authors: Heo
authors: Sang Kyu
authors: SK
authors: Kim
authors: Olesya
authors: O
authors: Kim
authors: Hye Kyung
authors: HK
authors: Kim
authors: Ji Young
authors: JY
authors: Yoon
authors: Hyoun Sook
authors: HS
authors: Kim
authors: Do Jin
authors: DJ
authors: Kim
authors: Sang Jae
authors: SJ
authors: Lee
authors: Hye Jin
authors: HJ
authors: Yoon
authors: Soon Jong
authors: SJ
authors: Kim
authors: Byung Gil
authors: BG
authors: Lee
authors: Hyun Kyu
authors: HK
authors: Song
authors: V Narry
authors: VN
authors: Kim
authors: Chung-Mo
authors: CM
authors: Park
authors: Se Won
authors: SW
authors: Suh
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000378:metabolism*; D004722:Endoribonucleases; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010454:Peptide Termination Factors / Q000737:chemistry; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D020871:RNA Stability; D012333:RNA, Messenger / Q000737:chemistry / Q000378:metabolism; D012260:Ribonucleases / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism*; D012996:Solutions; D040681:Structural Homology, Protein; D013379:Substrate Specificity; D013822:Thermoplasma / Q000201:enzymology*
chemical_list: D019843:Archaeal Proteins; D018797:Cell Cycle Proteins; C489002:ETF1 protein, human; D010454:Peptide Termination Factors; D012333:RNA, Messenger; D029701:Saccharomyces cerevisiae Proteins; D012996:Solutions; C112808:Dom34 protein, S cerevisiae; D004722:Endoribonucleases; D012260:Ribonucleases