Skip Navigation

Nucleic Acids Research 2006 34(13):3811-3818; doi:10.1093/nar/gkl517
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (495K) Freely available
Right arrow Screen PDF (503K) Freely available
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 ISI Web of Science
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 Search for citing articles in:
ISI Web of Science (10)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Minagawa, A.
Right arrow Articles by Nashimoto, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Minagawa, A.
Right arrow Articles by Nashimoto, M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Published online 11 August 2006

Nucleic Acids Research, 2006, Vol. 34, No. 13 3811-3818
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commerical use, distribution, and reproduction in any medium, provided the original work is properly cited.

Article

Identification by Mn2+ rescue of two residues essential for the proton transfer of tRNase Z catalysis

Asako Minagawa, Hiroaki Takaku, Ryohei Ishii1, Masamichi Takagi, Shigeyuki Yokoyama1,2,3 and Masayuki Nashimoto*

Department of Applied Life Sciences, Niigata University of Pharmacy and Applied Life Sciences Niigata, Niigata 956-8603, Japan 1 RIKEN Genomic Sciences Center Tsurumi, Yokohama 230-0045, Japan 2 RIKEN Harima Institute at SPring-8 Sayo-gun, Hyogo 679-5148, Japan 3 Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo Bunkyo-ku, Tokyo 113-0033, Japan

*To whom correspondence should be addressed. Tel: +81 250 25 5119; Fax: +81 250 25 5021; Email: mnashimoto{at}niigatayakudai.jp

Received May 17, 2006. Accepted July 6, 2006.

Thermotoga maritima tRNase Z cleaves pre-tRNAs containing the 74CCA76 sequence precisely after the A76 residue to create the mature 3' termini. Its crystal structure has revealed a four-layer {alpha}ß/ß{alpha} sandwich fold that is typically found in the metallo-ß-lactamase superfamily. The well-conserved six histidine and two aspartate residues together with metal ions are assumed to form the tRNase Z catalytic center. Here, we examined tRNase Z variants containing single amino acid substitutions in the catalytic center for pre-tRNA cleavage. Cleavage by each variant in the presence of Mg2+ was hardly detected, although it is bound to pre-tRNA. Surprisingly, however, Mn2+ ions restored the lost Mg2+-dependent activity with two exceptions of the Asp52Ala and His222Ala substitutions, which abolished the activity almost completely. These results provide a piece of evidence that Asp-52 and His-222 directly contribute the proton transfer for the catalysis.


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


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
K. Podzelinska, S.-M. He, M. Wathier, A. Yakunin, M. Proudfoot, B. Hove-Jensen, D. L. Zechel, and Z. Jia
Structure of PhnP, a Phosphodiesterase of the Carbon-Phosphorus Lyase Pathway for Phosphonate Degradation
J. Biol. Chem., June 19, 2009; 284(25): 17216 - 17226.
[Abstract] [Full Text] [PDF]

Home page
 GENES CELLSHome page
H. Takaku and M. Nashimoto
Escherichia coli tRNase Z can shut down growth probably by removing amino acids from aminoacyl-tRNAs
Genes Cells, November 1, 2008; 13(11): 1087 - 1097.
[Abstract] [Full Text] [PDF]


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.