The mitochondrial ATP synthase of chlorophycean algae contains eight subunits of unknown origin involved in the formation of an atypical stator-stalk and in the dimerization of the complex.
The mitochondrial ATP synthase of chlorophycean algae contains eight subunits of unknown origin involved in the formation of an atypical stator-stalk and in the dimerization of the complex.
复制标题
绿藻的线粒体 ATP 合酶含有八个来源不明的亚基，参与非典型定子茎的形成和复合物的二聚化。
DOI：
10.1007/s10863-006-9046-x
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发表时间：
2006
影响因子：
3
通讯作者：
González-Halphen,Diego
中科院分区：
文献类型：
--
作者：
Vázquez-Acevedo,Miriam;Cardol,Pierre;Cano-Estrada,Araceli;Lapaille,Marie;Remacle,Claire;González-Halphen,Diego
Mitochondrial F1FO-ATP synthase ofChlamydomonas reinhardtiiandPolytomella sp.is a dimer of 1,600,000 Da. InChlamydomonasthe enzyme lacks the classical subunits that constitute the peripheral stator-stalk as well as those involved in the dimerization of the fungal and mammal complex. Instead, it contains eight novel polypeptides named ASA1 to 8. We show that homologs of these subunits are also present in the chlorophycean algaePolytomellasp. andVolvox carterii. Blue Native Gel Electrophoresis analysis of mitochondria from different green algal species also indicates that stable dimeric mitochondrial ATP synthases may be characteristic of all Chlorophyceae. One additional subunit, ASA9, was identified in the purified mitochondrial ATP synthase ofPolytomellasp. The dissociation profile of thePolytomellaenzyme at high-temperatures and cross-linking experiments finally suggest that some of the ASA polypeptides constitute a stator-stalk with a unique architecture, while others may be involved in the formation of a highly-stable dimeric complex. The algal enzyme seems to have modified the structural features of its surrounding scaffold, while conserving almost intact the structure of its catalytic subunits.
