期刊
MOLECULAR BIOLOGY AND EVOLUTION
卷 27, 期 7, 页码 1630-1644出版社
OXFORD UNIV PRESS
DOI: 10.1093/molbev/msq049
关键词
chlamydomonas; algae; mitochondrial F1FO-ATP synthase; enzyme evolution; atypical subunits
资金
- Belgian Fonds pour la Recherche Scientifique (F.R.S.-FNRS) [1.C057.09, F.4735.06, 2.4638.05, 1.5.255.08, 2.4601.08]
- Action de la Recherche Concertee [ARC07/12-04]
- Belgian Science Policy
- CONACyT [56619, 203465]
- PAPIIT [IN217108]
- DGAPA
- UNAM (Mexico)
In yeast, mammals, and land plants, mitochondrial F1FO-ATP synthase (complex V) is a remarkable enzymatic machinery that comprises about 15 conserved subunits. Peculiar among eukaryotes, complex V from Chlamydomonadales algae (order of chlorophycean class) has an atypical subunit composition of its peripheral stator and dimerization module, with nine subunits of unknown evolutionary origin (Asa subunits). In vitro, this enzyme exhibits an increased stability of its dimeric form, and in vivo, Chlamydomonas reinhardtii cells are insensitive to oligomycins, which are potent inhibitors of proton translocation through the F-O moiety. In this work, we showed that the atypical features of the Chlamydomonadales complex V enzyme are shared by the other chlorophycean orders. By biochemical and in silico analyses, we detected several atypical Asa subunits in Scenedesmus obliquus (Sphaeropleales) and Chlorococcum ellipsoideum (Chlorococcales). In contrast, complex V has a canonical subunit composition in other classes of Chlorophytes (Trebouxiophyceae, Prasinophyceae, and Ulvophyceae) as well as in Streptophytes (land plants), and in Rhodophytes (red algae). Growth, respiration, and ATP levels in Chlorophyceae were also barely affected by oligomycin concentrations that affect representatives of the other classes of Chlorophytes. We finally studied the function of the Asa7 atypical subunit by using RNA interference in C. reinhardtii. Although the loss of Asa7 subunit has no impact on cell bioenergetics or mitochondrial structures, it destabilizes in vitro the enzyme dimeric form and renders growth, respiration, and ATP level sensitive to oligomycins. Altogether, our results suggest that the loss of canonical components of the complex V stator happened at the root of chlorophycean lineage and was accompanied by the recruitment of novel polypeptides. Such a massive modification of complex V stator features might have conferred novel properties, including the stabilization of the enzyme dimeric form and the shielding of the proton channel. In these respects, we discuss an evolutionary scenario for F1FO-ATP synthase in the whole green lineage (i.e., Chlorophyta and Streptophyta).
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