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

J. Biol. Chem., Vol. 283, Issue 34, 23333-23342, August 22, 2008

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 283/34/23333    most recent M710488200v1 Alert me when this article is cited 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 Google Scholar Articles by Keren, I. Articles by Ostersetzer-Biran, O. PubMed PubMed Citation Articles by Keren, I. Articles by Ostersetzer-Biran, O. Social Bookmarking                      What's this?

Characterization of the Molecular Basis of Group II Intron RNA Recognition by CRS1-CRM Domains^*

From the Institute of Plant Sciences, Agricultural Research Organization, Bet Dagan 50250, Israel

CRM (chloroplast RNA splicing and ribosome maturation) is a recently recognized RNA-binding domain of ancient origin that has been retained in eukaryotic genomes only within the plant lineage. Whereas in bacteria CRM domains exist as single domain proteins involved in ribosome maturation, in plants they are found in a family of proteins that contain between one and four repeats. Several members of this family with multiple CRM domains have been shown to be required for the splicing of specific plastidic group II introns. Detailed biochemical analysis of one of these factors in maize, CRS1, demonstrated its high affinity and specific binding to the single group II intron whose splicing it facilitates, the plastid-encoded atpF intron RNA. Through its association with two intronic regions, CRS1 guides the folding of atpF intron RNA into its predicted "catalytically active" form. To understand how multiple CRM domains cooperate to achieve high affinity sequence-specific binding to RNA, we analyzed the RNA binding affinity and specificity associated with each individual CRM domain in CRS1; whereas CRM3 bound tightly to the RNA, CRM1 associated specifically with a unique region found within atpF intron domain I. CRM2, which demonstrated only low binding affinity, also seems to form specific interactions with regions localized to domains I, III, and IV. We further show that CRM domains share structural similarities and RNA binding characteristics with the well known RNA recognition motif domain.

Received for publication, December 24, 2007 , and in revised form, May 23, 2008.

^* This work was supported by grants from the German-Israeli Foundation for Scientific Research and Development, Young Scientist Grant GIF 2102/2004 (to O. O.-B.), and United States-Israel Binational Agricultural Research and Development Fund Grant IS-374-05 (to O. O.-B.). 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 Tables S1 and S2 and Figs. S1-S3.

¹ Both authors contributed equally to this work.

² Present address: Dept. of Structural Biology, Weizmann Institute, Rehovot 76100, Israel.

³ To whom correspondence should be addressed: Agricultural Research Organization, P.O. Box 6, Bet-Dagan 50250, Israel. Tel.: 972-3-968-3397; Fax: 972-3-966-9583; E-mail: biranos{at}volcani.agri.gov.il.

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