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Molecular Plant Advance Access originally published online on October 11, 2009
Molecular Plant 2009 2(6):1397-1409; doi:10.1093/mp/ssp079
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© The Author 2009. Published by the Molecular Plant Shanghai Editorial Office in association with Oxford University Press on behalf of CSPP and IPPE, SIBS, CAS.

In vivo Studies on the Roles of Tic55-Related Proteins in Chloroplast Protein Import in Arabidopsis thaliana

Patrik Boija, Ramesh Patelb, Christel Garciaa, Paul Jarvisb,1 and Henrik Aronssona,1

a Department of Plant and Environmental Sciences, University of Gothenburg, Box 461, SE-405 30 Gothenburg, Sweden
b Department of Biology, University of Leicester, University Road, Leicester LE1 7RH, UK

1 To whom correspondence should be addressed. E-mail henrik.aronsson{at}dpes.gu.se, fax 46-317862560, tel. 46-317864802.

1 To whom correspondence should be addressed. E-mail rpj3{at}le.ac.uk, fax 44-1162523330, tel. 44-1162231296.

The Tic55 (Translocon at the inner envelope membrane of chloroplasts, 55 kDa) protein was identified in pea as a putative regulator, possibly linking chloroplast protein import to the redox state of the photosynthetic machinery. Two Tic55 homologs have been proposed to exist in Arabidopsis: atTic55-II and AtPTC52 (Protochlorophyllide-dependent Translocon Component, 52 kDa; has also been called atTic55-IV). Our phylogenetic analysis shows that atTic55-II is an ortholog of psTic55 from pea (Pisum sativum), and that AtPTC52 is a more distant homolog of the two. AtPTC52 was included in this study to rule out possible functional links between the proteins in Arabidopsis. No detectable mutant phenotypes were found in two independent T-DNA knockout mutant plant lines for each Arabidopsis protein, when compared with wild-type: visible appearance, chlorophyll content, photosynthetic performance, and chloroplast protein import, for example, were all normal. Both wild-type and tic55-II mutant chloroplasts exhibited deficient protein import when treated with diethylpyrocarbonate, indicating that Tic55 is not the sole target of this reagent in relation to protein import. Furthermore, ptc52 mutant chloroplasts were not defective with respect to pPORA import, which was previously reported to involve PTC52 in barley. Thus, we conclude that atTic55-II and AtPTC52 are not strictly required for functional protein import in Arabidopsis.

Key Words: Arabidopsis • chloroplast • import • protein targeting • Tic55


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