Cloned (Comment) | Organism |
---|---|
phylogenetic analysis | Chlamydomonas reinhardtii |
phylogenetic analysis | Tetradesmus obliquus |
phylogenetic analysis | Chlorococcum ellipsoideum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | in vivo, Chlamydomonas reinhardtii cells are insensitive to oligomycins, which are potent inhibitors of proton translocation through the FO moiety. Subunit Asa7 plays a role in the sensitivity to oligomycin | Chlamydomonas reinhardtii | |
additional information | in vivo, Chlamydomonas reinhardtii cells are insensitive to oligomycins, which are potent inhibitors of proton translocation through the FO moiety | Chlorococcum ellipsoideum | |
additional information | in vivo, Chlamydomonas reinhardtii cells are insensitive to oligomycins, which are potent inhibitors of proton translocation through the FO moiety | Tetradesmus obliquus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrial membrane | - |
Chlamydomonas reinhardtii | 31966 | - |
mitochondrial membrane | - |
Tetradesmus obliquus | 31966 | - |
mitochondrial membrane | - |
Chlorococcum ellipsoideum | 31966 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Chlamydomonas reinhardtii | - |
cw15 arg7-8 mt+ mutant | - |
Chlorococcum ellipsoideum | - |
- |
- |
Tetradesmus obliquus | - |
- |
- |
Subunits | Comment | Organism |
---|---|---|
dimer | complex V exhibits an increased stability of its dimeric form | Chlamydomonas reinhardtii |
dimer | complex V exhibits an increased stability of its dimeric form | Tetradesmus obliquus |
dimer | complex V exhibits an increased stability of its dimeric form | Chlorococcum ellipsoideum |
Synonyms | Comment | Organism |
---|---|---|
complex V | - |
Chlamydomonas reinhardtii |
complex V | - |
Tetradesmus obliquus |
complex V | - |
Chlorococcum ellipsoideum |
mitochondrial F1Fo-ATP synthase | - |
Chlamydomonas reinhardtii |
mitochondrial F1Fo-ATP synthase | - |
Tetradesmus obliquus |
mitochondrial F1Fo-ATP synthase | - |
Chlorococcum ellipsoideum |
General Information | Comment | Organism |
---|---|---|
evolution | 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, i.e. Asa subunits. The loss of canonical components of the complex V stator happened at the root of chlorophycean lineage and is 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 | Chlamydomonas reinhardtii |
evolution | among eukaryotes, complex V from Chlorococcales algae (order of chlorophycean class) has an atypical subunit composition of its peripheral stator and dimerization module, with nine subunits of unknown evolutionary origin, i.e. Asa subunits. The loss of canonical components of the complex V stator happened at the root of chlorophycean lineage and is 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 | Chlorococcum ellipsoideum |
evolution | among eukaryotes, complex V from Sphaeropleales algae (order of chlorophycean class) has an atypical subunit composition of its peripheral stator and dimerization module, with nine subunits of unknown evolutionary origin, i.e. Asa subunits. The loss of canonical components of the complex V stator happened at the root of chlorophycean lineage and is 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 | Tetradesmus obliquus |
malfunction | loss of Asa7 atypical subunit in Chlamydomonas reinhardtii leads to an unstable complex V and increased sensitivity to oligomycin impared to the wild-type | Chlamydomonas reinhardtii |