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Literature summary for 7.1.2.2 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
Search for more literature for 7.1.2.2

Cloned(Commentary)

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

Inhibitors

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

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

Organism

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

Subunits

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

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

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