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Nucleic Acids Research 2006 34(1):386-394; doi:10.1093/nar/gkj433
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Published online 12 January 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

Article

Translation of chloroplast psbD mRNA in Chlamydomonas is controlled by a secondary RNA structure blocking the AUG start codon

Birgit Klinkert, Ingolf Elles and Jörg Nickelsen*

Allgemeine und Molekulare Botanik, Ruhr-Universität Bochum, Universitätsstr. 150 D-44780 Bochum, Germany

*To whom correspondence should be addressed. Tel: 0049 234 3224247; Fax: 0049 234 3214184; Email: joerg.nickelsen{at}rub.de

Received November 3, 2005. Revised December 21, 2005. Accepted December 21, 2005.

Translation initiation represents a key step during regulation of gene expression in chloroplasts. Here, we report on the identification and characterization of three suppressor point mutations which overcome a translational defect caused by the deletion of a U-rich element in the 5'-untranslated region (5'-UTR) of the psbD mRNA in the green alga Chlamydomonas reinhardtii. All three suppressors affect a secondary RNA structure encompassing the psbD AUG initiation codon within a double-stranded region as judged by the analysis of site-directed chloroplast mutants as well as in vitro RNA mapping experiments using RNase H. In conclusion, the data suggest that these new element serves as a negative regulator which mediates a rapid shut-down of D2 synthesis.


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