Evidence that mitochondrial isozymes are genetically less variable than cytoplasmic isozymes

Abstract

SummaryIt has been proposed that isoenzymes functioning within cell organelles (chloroplasts, mitochondria) are genetically less variable than their cytoplasmic counterparts, as a result either of constraints imposed by the need to cross organelle membranes or from the different and specialized nature of organelle metabolism. However, some recent findings concerning chloroplast and cytoplasmic isozyme variability are not consistent with this thesis. We have analyzed a number of surveys of electrophoretically detectable enzyme variation in vertebrates, and show that for each of the four tested enzymes (malate dehydrogenase, isocitrate dehydrogenase, malic enzyme, and aspartate aminotransferase), the mitochondrial isozymes are less variable than their corresponding cytosplasmic forms. The mean heterozygosities across the four enzymes are 0·083 and 0·038 for the cytoplasmic and mitochondrial forms respectively. We conclude that mitochondrial isozymes are indeed subject to greater constraints than cytoplasmic forms and have fewer sites able to accept neutral or slightly deleterious mutations. It is also noted that of the enzymes analyzed, that with the smallest subunit molecular weight (MDH) has the least variable cytoplasmic and mitochondrial isozymes, whereas the enzyme with the largest subunits (ME) has the most variable isozymes.