Structural and functional insights into Dom34, a key component of no-go mRNA decay

Cited 78 time in Web of Science Cited 78 time in Scopus

Lee, Hyung Ho; Kim, Youn-Sung; Kim, Kyoung Hoon; Heo, Inha; Kim, Sang Kyu; Kim, Olesya; Kim, Hye Kyung; Yoon, Ji Young; Kim, Hyoun Sook; Kim, Do Jin; Lee, Sang Jae; Yoon, Hye Jin; Kim, Soon Jong; Lee, Byung Gil; Song, Hyun Kyu; Kim, V. NarryPark, Chung-Mo; Suh, Se Won

Issue Date
Cell Press
Molecular Cell, Vol.27 No.6, pp.938-950
The yeast protein Dom34 is a key component of no-go decay, by which rnRNAs 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.
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College of Natural Sciences (자연과학대학)Dept. of Biological Sciences (생명과학부)Journal Papers (저널논문_생명과학부)
College of Natural Sciences (자연과학대학)Dept. of Chemistry (화학부)Journal Papers (저널논문_화학부)
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