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.
Original language | English |
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Pages (from-to) | 938-950 |
Number of pages | 13 |
Journal | Molecular Cell |
Volume | 27 |
Issue number | 6 |
DOIs | |
Publication status | Published - 2007 Sept 21 |
Bibliographical note
Funding Information:We thank the beamline staffs for assistance during data collection (BL-4A and BL-6B of Pohang Light Source, Korea, and BL-5A of Photon Factory, Japan). This work was supported by the Korea Ministry of Science and Technology (New Drug Target Discovery Research Grant to S.W.S.).
Keywords
- RNA
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology