Abstract
The ribosomal proteins of several species within the genus Podospora have been analyzed by two-dimensional polyacrylamide gel electrophoresis. Differences in the migration of four proteins of the large subunit have been found between the two hybridizable species Podospora anserina and P. comata. Haploid offspring of this interspecific cross show all possible combinations of ribosomal proteins from both species. Therefore, the homologous proteins are functionally interchangeable. Moreover, the sizes of the different classes of offspring show that the genes encoding the four ribosomal proteins L2, L13, L16, and L20 are not clustered.