Structural highlights
Function
[CDAT8_METKA] Catalyzes the deamimation of cytosine to uracil at position 8 of tRNA in 30 different tRNAs. This editing guarantees the proper folding and functionality of the tRNAs.[1]
Publication Abstract from PubMed
All canonical transfer RNAs (tRNAs) have a uridine at position 8, involved in maintaining tRNA tertiary structure. However, the hyperthermophilic archaeon Methanopyrus kandleri harbors 30 (out of 34) tRNA genes with cytidine at position 8. Here, we demonstrate C-to-U editing at this location in the tRNA's tertiary core, and present the crystal structure of a tRNA-specific cytidine deaminase, CDAT8, which has the cytidine deaminase domain linked to a tRNA-binding THUMP domain. CDAT8 is specific for C deamination at position 8, requires only the acceptor stem hairpin for activity, and belongs to a unique family within the "cytidine deaminase-like" superfamily. The presence of this C-to-U editing enzyme guarantees the proper folding and functionality of all M. kandleri tRNAs.
A cytidine deaminase edits C to U in transfer RNAs in Archaea.,Randau L, Stanley BJ, Kohlway A, Mechta S, Xiong Y, Soll D Science. 2009 May 1;324(5927):657-9. PMID:19407206[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Randau L, Stanley BJ, Kohlway A, Mechta S, Xiong Y, Soll D. A cytidine deaminase edits C to U in transfer RNAs in Archaea. Science. 2009 May 1;324(5927):657-9. PMID:19407206 doi:324/5927/657
- ↑ Randau L, Stanley BJ, Kohlway A, Mechta S, Xiong Y, Soll D. A cytidine deaminase edits C to U in transfer RNAs in Archaea. Science. 2009 May 1;324(5927):657-9. PMID:19407206 doi:324/5927/657
