Question

is it surprising that there is COX6-BIO present in a mutant strain of Yeast compared to its wild type? why or why not

Answer 1

Answer-

According to the given question-

COX6- Electron transport chain of mitochondria have four enzyme complexes such as cytochrome c oxidase, NADH dehydrogenase, coenzyme Q cytochrome c reductase, and succinate dehydrogenase. the chain also have coenzyme Q and cytochrome c. In yeart these proteins are encoded by genes present in nucleus.   The gene COX6 coded cytochrome c oxidase enzyme having subunit VI.

• Atp9p ring is present in the mitochondrial ATP synthase of yeast which helps in proton translocation for synthesis as well as hydrolysis of ATP molecule.
• Atp9p is also present in the three protein complex  as well as with Cox6p. more Atp9p is present in as form of ring in wild type yeast than the mutant yeast.  
• The mutation in atp10 responsible for blocking the  interaction between the Atp9p ring to the and other component of  ATP synthase. Due to this reason the ring that are formed in a cox6 mutant are reduced because Cox6p play an important role in oligomerization of Atp9p.
• Atp9p interact with F1 ATPase after oligomerization  to form the ring. After interaction thay form F1-Atp9p ring which combine with the other component such as Atp6p, Atp8p, except OSCP. Cox6p and Atp9p are responsible for formation of ATP synthase and COX respectively.
• Atp9p oligomerization to form ring  in ox6 mutant mitochondria are less effective that the wild type when compared to study the effect under glucose-repressed conditions.
• cox6 mutant have less Atp9p which are associated with ring in cox6 that are new translated and their assembly of ring are also less efficient than the wild type because Cox6p helps in assembling of ATP synthase enzyme and this is responsible for increaing the efficiency of ring formation.