Evolution of proteins in mammalian cytoplasmic and mitochondrial ribosomes.

The proteins of cytoplasmic and mitochondrial ribosomes from the cow and the rat were analyzed by co-electrophoresis in two dimensional polyacrylamide gels to determine their relative evolutionary rates. In a pairwise comparison of individual ribosomal proteins (r-proteins) from the cow and the rat, over 85% of the cytoplasmic r-proteins have conserved electrophoretic properties in this system, while only 15% of the proteins of mitochondrial ribosomes from these animals fell into this category. These values predict that mammalian mitochondrial r-proteins are evolving about 13 times more rapidly than cytoplasmic r-proteins. Based on actual evolutionary rates for representative cytoplasmic r-proteins, this mitochondrial r-protein evolutionary rate corresponds to an amino acid substitution rate of 40 X 10(-10) per site per year, placing mitochondrial r-proteins in the category of rapidly evolving proteins. The mitochondrial r-proteins are apparently evolving at a rate comparable to that of the mitochondrial rRNA, suggesting that functional constraints act more or less equally on both kinds of molecules in the ribosome. It is significant that mammalian mitochondrial r-proteins are evolving more rapidly than cytoplasmic r-proteins in the same cell, since both sets of r-proteins are encoded by nuclear genes. Such a difference in evolutionary rates implies that the functional constraints operating on ribosomes are somewhat relaxed for mitochondrial ribosomes.

Protein composition of the bovine mitochondrial ribosome.

The protein complement of the bovine mitochondrial ribosome has been analyzed by two-dimensional electrophoresis in polyacrylamide gels to determine the number and molecular weights of the ribosomal proteins. Salt-washed ribosomal subunits are found to contain a total of 85 ribosomal proteins, 84 of which are electrophoretically distinct between the two subunits. These proteins are also electrophoretically distinguished from those of cytoplasmic ribosomes. This large number of proteins does not appear to be due to contamination by cytoplasmic ribosomal proteins or by adherent nonribosomal proteins. The molecular weights of these proteins are considerably larger than those of Escherichia coli ribosomal proteins, and are similar to those of bovine cytoplasmic ribosomal proteins. The sum of the molecular weights of the 85 proteins agrees well with that predicted by physical chemical measurements of the total mass of protein in the two subunits. Bovine mitochondrial ribosomes thus contain about twice as much protein as RNA, a highly unusual composition in comparison to the other kinds of ribosomes which have been characterized to date. In addition, it appears that the ribosomal proteins themselves are less basic than the proteins of most other ribosomes.