Protein carboxyl-methylation in rat testes: a study of inherited and X-ray-induced seminiferous tubule failure.
Protein carboxyl-methylase (PCM), the enzyme that transfers methyl groups from S-adenosyl-methionine to free carboxyl groups on proteins, is highly localized in testes. The cellular distribution of PCM and its substrates, the methyl acceptor proteins, was investigated. Separation of testicular cells on an albumin gravity gradient revealed the preferential localization of both enzyme and substrates in spermatids. In young rats, PCM activity increases with age coincidently with germ cell maturation. Rats which are heterozygous for the Hre gene (Hre/+) are infertile as a result of germ cell depletion. In these animals, testicular PCM specific activity and total activity were, respectively, 4--6 and 40--50 times lower than in normal testes. Enzyme activity in testes from animals with x-ray-induced germ cell depletion was also very low. These observations suggest that PCM is located in germ cells.
D000818:Animals; D006579:Heterozygote; D007248:Infertility, Male / Q000201:enzymology; D008297:Male; D011496:Protein Methyltransferases / Q000378:metabolism*; D011497:Protein O-Methyltransferase / Q000378:metabolism*; D051381:Rats; D012671:Seminiferous Tubules / Q000201:enzymology / Q000528:radiation effects*; D013737:Testis / Q000378:metabolism* / Q000528:radiation effects*
D011496:Protein Methyltransferases; D011497:Protein O-Methyltransferase