Publications
Detailed Information
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
- Authors
- Issue Date
- 2007-09
- Publisher
- Cell Press
- Citation
- Molecular Cell, Vol.27 No.6, pp.938-950
- Abstract
- 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.
- ISSN
- 1097-2765
- Files in This Item:
- There are no files associated with this item.
Item View & Download Count
Items in S-Space are protected by copyright, with all rights reserved, unless otherwise indicated.