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Literature summary extracted from

  • Lapaille, M.; Escobar-Ramirez, A.; Degand, H.; Baurain, D.; Rodriguez-Salinas, E.; Coosemans, N.; Boutry, M.; Gonzalez-Halphen, D.; Remacle, C.; Cardol, P.
    Atypical subunit composition of the chlorophycean mitochondrial F1FO-ATP synthase and role of Asa7 protein in stability and oligomycin resistance of the enzyme (2010), Mol. Biol. Evol., 27, 1630-1644.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.1.2.2 phylogenetic analysis Chlamydomonas reinhardtii
7.1.2.2 phylogenetic analysis Tetradesmus obliquus
7.1.2.2 phylogenetic analysis Chlorococcum ellipsoideum

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.1.2.2 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
7.1.2.2 additional information in vivo, Chlamydomonas reinhardtii cells are insensitive to oligomycins, which are potent inhibitors of proton translocation through the FO moiety Chlorococcum ellipsoideum
7.1.2.2 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

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.2.2 mitochondrial membrane
-
 Chlamydomonas reinhardtii 31966
-
7.1.2.2 mitochondrial membrane
-
 Tetradesmus obliquus 31966
-
7.1.2.2 mitochondrial membrane
-
 Chlorococcum ellipsoideum 31966
-

Organism

EC Number Organism UniProt Comment Textmining
7.1.2.2 Chlamydomonas reinhardtii
-
 cw15 arg7-8 mt+ mutant
-
7.1.2.2 Chlorococcum ellipsoideum
-
-
-
7.1.2.2 Tetradesmus obliquus
-
-
-

Subunits

EC Number Subunits Comment Organism
7.1.2.2 dimer complex V exhibits an increased stability of its dimeric form Chlamydomonas reinhardtii
7.1.2.2 dimer complex V exhibits an increased stability of its dimeric form Tetradesmus obliquus
7.1.2.2 dimer complex V exhibits an increased stability of its dimeric form Chlorococcum ellipsoideum

Synonyms

EC Number Synonyms Comment Organism
7.1.2.2 complex V
-
 Chlamydomonas reinhardtii
7.1.2.2 complex V
-
 Tetradesmus obliquus
7.1.2.2 complex V
-
 Chlorococcum ellipsoideum
7.1.2.2 mitochondrial F1Fo-ATP synthase
-
 Chlamydomonas reinhardtii
7.1.2.2 mitochondrial F1Fo-ATP synthase
-
 Tetradesmus obliquus
7.1.2.2 mitochondrial F1Fo-ATP synthase
-
 Chlorococcum ellipsoideum

General Information

EC Number General Information Comment Organism
7.1.2.2 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
7.1.2.2 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
7.1.2.2 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
7.1.2.2 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