期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 511, 期 2, 页码 228-233出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2019.01.142
关键词
tRNA; Glycyl-tRNA synthetase; Nanoarchaeum equitans; Crystal structure; Acceptor-stem recognition; Aminoacylation
资金
- Ministry of Education, Culture, Sports, Science and Technology, Japan (MEXT) [17K19210]
- Grants-in-Aid for Scientific Research [17K19210] Funding Source: KAKEN
This study reports the X-ray crystallographic structure of the glycyl-tRNA synthetase (GlyRS) of Nanoarchaeum equitans - a hyperthermophilic archaeal species. This is the first archaeal GlyRS crystal structure elucidated. The GlyRS comprises an N-terminal catalytic domain and a C-terminal anticodon-binding domain with a long beta-sheet inserted between these domains. An unmodified transcript of the wild-type N. equitans tRNA(Gly) was successfully glycylated using GlyRS. Substitution of the discriminator base A73 of tRNA(Gly) with any other nucleotide caused a significant decrease in glycylation activity. Mutational analysis of the second base-pair C2G71 of the acceptor stem of tRNA(Gly) elucidated the importance of the base-pair, especially G71, as an identity element for recognition by GlyRS. Glycylation assays using tRNA(Gly) G71 substitution mutants and a GlyRS mutant where Arg223 is mutated to alanine strengthen the possibility that the carbonyl oxygen at position 6 of G71 would hydrogen-bond with the guanidine nitrogen of Arg223 in N. equitans GlyRS. (C) 2019 Elsevier Inc. All rights reserved.
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