Skip Navigation



Journal of Biochemistry Advance Access published online on January 29, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp020
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow All Versions of this Article:
145/5/635    most recent
mvp020v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Tsuchiya, W.
Right arrow Articles by Hasegawa, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tsuchiya, W.
Right arrow Articles by Hasegawa, T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Molecular Recognition of Tryptophan tRNA by Tryptophanyl-tRNA Synthetase from Aeropyrum pernix K1

Wataru Tsuchiya1 and Tsunemi Hasegawa1,2,*

1Graduate School of Science and Engineering, Yamagata University, Yamagata 990-8560 and 2Department of Material and Biological Chemistry, Faculty of Science, Yamagata University, Yamagata 990-8560, Japan

*To whom correspondence should be addressed: Tsunemi Hasegawa, Tel/Fax: +81-23-628-4604, E-mail: hasegawa{at}sci.kj.yamagata-u.ac.jp

Received December 17, 2008; Accepted January 22, 2009


  Abstract

The identity elements of transfer RNA are the molecular basis for recognition by each cognate aminoacyl-tRNA synthetase. In the archaea system, the tryptophan tRNA identity has not been determined in detail. To investigate the molecular recognition mechanism of tryptophan tRNA by tryptophanyl-tRNA synthetase (TrpRS) from the hyperthermophilic and aerobic archaeon, Aeropyrum pernix K1, various mutant transcripts of tryptophan tRNA prepared by an in vitro transcription system were examined by overexpression of A. pernix TrpRS. Substitution of the discriminator base, A73, impaired tryptophan incorporation activity. Changing the G1-C72 base pair to other base pairs also decreased the aminoacylation activity. Substitutions of anticodon CCA revealed that the C34 and C35 mutants dramatically reduced aminoacylation with tryptophan, but the A36 mutants had the same activity as the wild-type. The results indicate that the anticodon nucleotides C34, C35, discriminator base A73 and G1-C72 base pair are major recognition sites for A. pernix TrpRS.

Key Words: tRNA identity, Tryptophan tRNA, Tryptophanyl-tRNA synthetase, Archaea, Aeropyrum pernix K1


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.