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Nucleic Acids Research 2004 32(11):3503-3510; doi:10.1093/nar/gkh682
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Published online 30 June 2004

Nucleic Acids Research, Vol. 32 No. 11 © Oxford University Press 2004; all rights reserved

Multiple elements required for translation of plastid atpB mRNA lacking the Shine-Dalgarno sequence

Tetsuro Hirose1 and Masahiro Sugiura1,2,*

1 Center for Gene Research, Nagoya University, Nagoya 464-8602, Japan and 2 Graduate School of Natural Sciences, Nagoya City University, Yamanohata, Mizuho, Nagoya 467-8501, Japan

* To whom correspondence shoud be addressed at Graduate School of Natural Sciences, Nagoya City University, Yamanohata, Mizuho, Nagoya 467-8501, Japan. Tel/Fax: +81 52 872 6021; Email: sugiura{at}nsc.nagoya-cu.ac.jp

Received April 2, 2004; Revised and Accepted June 16, 2004

The mechanism of translational initiation differs between prokaryotes and eukaryotes. Prokaryotic mRNAs generally contain within their 5'-untranslated region (5'-UTR) a Shine-Dalgarno (SD) sequence that serves as a ribosome-binding site. Chloroplasts possess prokaryotic-like translation machinery, and many chloroplast mRNAs have an SD-like sequence, but its position is variable. Tobacco chloroplast atpB mRNAs contain no SD-like sequence and are U-rich in the 5'-UTR (–20 to –1 with respect to the start codon). In vitro translation assays with mutated mRNAs revealed that an unstructured sequence encompassing the start codon, the AUG codon and its context are required for translation. UV crosslinking experiments showed that a 50 kDa protein (p50) binds to the 5'-UTR. Insertion of an additional initiation region (SD-sequence and AUG) in the 5'-UTR, but not downstream, arrested translation from the authentic site; however, no inhibition was observed by inserting only an AUG triplet. We hypothesize for translational initiation of the atpB mRNA that the ribosome enters an upstream region, slides to the start codon and forms an initiation complex with p50 and other components.


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