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

Journal Article · Thu Jan 01 00:00:00 EST 2009 · Science

DOI:https://doi.org/10.1126/science.1170123· OSTI ID:979977

Randau, L; Stanley, B; Kohlway, A; Mechta, S; Xiong, Y; Söll, D

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.

• Research Organization: Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: DE-AC02-98CH10886
• OSTI ID: 979977
• Report Number(s): BNL-92895-2010-JA; SCEHDK; TRN: US201015%%1362
• Journal Information: Science, Vol. 324; ISSN 0193-4511
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
CRYSTAL STRUCTURE
CYTIDINE
DEAMINATION
ENZYMES
GENES
HARBORS
TRANSFER RNA
URIDINE
national synchrotron light source