HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 279, Issue 1, 540-546, January 2, 2004

This Article Full Text Full Text (PDF) All Versions of this Article: 279/1/540    most recent M305499200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Ohuchi, S. J. Articles by Inoue, T. Search for Related Content PubMed PubMed Citation Articles by Ohuchi, S. J. Articles by Inoue, T. Social Bookmarking                      What's this?

Artificial Modules for Enhancing Rate Constants of a Group I Intron Ribozyme without a P4-P6 Core Element^*

Shoji J. Ohuchi, Yoshiya Ikawa, Hideaki Shiraishi, and Tan Inoue¶

From the Graduate School of Science and Graduate School of Biostudies, Kyoto University, Kyoto 606-8502, Japan

In this paper we report newly selected artificial modules that enhance the k_cat values comparable with or higher than those of the wild-type ribozyme with broad substrate specificity. The elements required for the catalysis of Group I intron ribozymes are concentrated in the P3-P7 domain of their core region, which consists of two conserved helical domains, P4-P6 and P3-P7. Previously, we reported the in vitro selection of artificial modules residing at the peripheral region of a mutant Group I ribozyme lacking P4-P6. We found that derivatives of the ribozyme containing the modules performed the reversal of the first step of the self-splicing reaction efficiently by using their affinity to the substrate RNA, although their k_cat values and substrate specificity were uninfluenced and limited, respectively. The results show that it is possible to add a variety of new domains at the peripheral region that play a role comparable with that of the conserved P4-P6 domain.

Received for publication, May 27, 2003 , and in revised form, October 6, 2003.

^* This work was supported by grants-in-aid for Scientific Research on Priority Areas (to T. I.), the Encouragement of Young Scientists (to Y. I.) from the Ministry of Education, Science, Sports, and Culture, Japan, and Takeda Science Foundation (to T. I.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains Supplemental Figs. 1-5.

^¶ To whom correspondence should be addressed. E-mail: tan{at}kuchem.kyoto-u.ac.jp.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				Y. Ikawa, T. Shiohara, S. Ohuchi, and T. Inoue Concerted Effects of Two Activator Modules on the Group I Ribozyme Reaction J. Biochem., April 1, 2009; 145(4): 429 - 435. [Abstract] [Full Text] [PDF]

				N. Kim, H. H. Gan, and T. Schlick A computational proposal for designing structured RNA pools for in vitro selection of RNAs RNA, April 1, 2007; 13(4): 478 - 492. [Abstract] [Full Text] [PDF]

				J. GEVERTZ, H. H. GAN, and T. SCHLICK In vitro RNA random pools are not structurally diverse: A computational analysis RNA, June 1, 2005; 11(6): 853 - 863. [Abstract] [Full Text] [PDF]