Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2050490 | FEBS Letters | 2007 | 7 Pages |
Abstract
The precursor protein receptor at the chloroplast outer membrane atToc33 is a GTPase, which can be inactivated by phosphorylation in vitro, being arrested in the GDP loaded state. To assess the physiological function of phosphorylation, attoc33 knock out mutants were complemented with a mutated construct mimicking the constitutively phosphorylated state. Our data suggest that the reduced functionality of the mutant protein can be compensated by its upregulation. Chloroplast biogenesis and photosynthetic activity are impaired in the mutants during the early developmental stage, which is consistent with the requirement of atToc33 in young photosynthetic tissues.
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Authors
Mislav Oreb, Mikael Zoryan, Aleksandar Vojta, Uwe G. Maier, Lutz A. Eichacker, Enrico Schleiff,