THE UNUSUAL REVERSION PROPERTIES OF A MITOCHONDRIAL MUTATION IN THE STRUCTURAL GENE OF SUBUNIT-I OF CYTOCHROME-OXIDASE OF SACCHAROMYCES-CEREVISIAE REVEAL A PROBABLE HISTIDINE LIGAND OF THE REDOX CENTER

We have analyzed a mutation in the mitochondrial gene oxi3 coding for subunit I of cytochrome-oxidase in the yeast Saccharomyces cerevisiae. This mutation replaces one of the seven invariant histidines of the polypeptide (position 378) by a tyrosine, and leads to a respiratory deficient phenotype. A total of 157 revertants, which have recovered the ability to grow on a respiratory substrate, have been selected from this mutant (tyrosine 378). The nature of the reversion has been analysed by a rapid screening procedure and 32 of the revertants have been sequenced. They are all true back-mutations reintroducing the histidine in position 378. This very exceptional situation suggests that this histidine is a ligand of the redox center of cytochrome oxidase.