A Cytidine Deaminase Edits C to U in Transfer RNAs in Archaea

被引:55
作者
Randau, Lennart [1 ]
Stanley, Bradford J. [1 ]
Kohlway, Andrew [1 ]
Mechta, Sarah [1 ]
Xiong, Yong [1 ]
Soll, Dieter [1 ,2 ]
机构
[1] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA
[2] Yale Univ, Dept Chem, New Haven, CT 06520 USA
关键词
CRYSTAL-STRUCTURE; ADENOSINE-DEAMINASE; FUNCTIONAL IMPLICATIONS; METHANOPYRUS-KANDLERI; ESCHERICHIA-COLI; GENETIC ELEMENTS; DOMAIN; 4-THIOURIDINE; APOBEC3G; INOSINE;
D O I
10.1126/science.1170123
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:657 / 659
页数:3
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