SUMMARYAtFtsH4 is one of four inner membrane-bound mitochondrial ATP-dependent metalloproteases in Arabidopsis thaliana, called AAA proteases, whose catalytic site is exposed to the intermembrane space. In the present study, we used a reverse-genetic approach to investigate the physiological role of the AtFtsH4 protease. We found that loss of AtFtsH4 did not significantly affect Arabidopsis growth under optimal conditions (long days); however, severe morphological and developmental abnormalities in late rosette development occurred under short-day conditions. The asymmetric shape and irregular serration of expanding leaf blades were the most striking features of the ftsh4 mutant phenotype. The severe abnormal morphology of the leaf blades was accompanied by ultrastructural changes in mitochondria and chloroplasts. These abnormalities correlated with elevated levels of reactive oxygen species and carbonylated mitochondrial proteins. We found that two classes of molecular chaperones, Hsp70 and prohibitins, were over-expressed in ftsh4 mutants during late vegetative growth under both short-and long-day conditions. Taken together, our data indicate that lack of AtFtsH4 results in impairment of organelle development and Arabidopsis leaf morphology under short-day conditions.
The Arabidopsis genome encodes four mitochondrially localized adenosine 5#-triphosphate-dependent metalloproteases called FtsH or AAA proteases. All of them span the inner mitochondrial membrane but the catalytic site of two of them (AtFtsH4 and AtFtsH11) faces the intermembrane space, while AtFtsH3 and AtFtsH10 face the matrix. We used a combination of blue-native polyacrylamide gel electrophoresis and histochemical staining to reveal the consequences of the loss of one of mitochondrial FtsHs on the efficiency of the oxidative phosphorylation system in Arabidopsis mitochondria. To address this issue, we have selected homozygous lines of respective transferred DNA (T-DNA) insertional mutants. A decrease in the activity of complexes I and V but not complex IV was observed in the ftsh mutants, except for the mutant lacking functional FtsH11. The reduced activity of complexes I and V was well correlated with a decreased protein level of these complexes. Western blots experiments using specific antibodies against complex V subunits showed a significant reduction of these subunits only in the ftsh4 mutant. Taken together, our results reveal a role of FtsH3, FtsH4 and FtsH10 proteases in the biogenesis of a plant oxidative phosphorylation system.
The atp6 gene has been identified as a single-copy sequence in the mitochondrial genome of the pea. An unexpected finding concerns the atp6 5' extension which is known to be poorly conserved at the sequence level, even between closely related plant species. We have shown that the presequences of ATP6 from the pea and other species belonging to the Vicieae tribe of Fabaceae (broad bean, hairy vetch) share a sequence similarity which extends to long 5' untranslated transcript termini. The reason for the observed conservation is not clear but may simply reflect the close phylogenetic relationship of species from the Vicieae tribe. The result of editing analysis indicates the occurrence of fully and partially edited transcripts of atp6 in the pea mitochondria. The majority of the editing sites are targeted to the last transmembrane domain of the pea ATP6, important in proton translocation and interactions with other subunits of ATP synthase.
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