Kotusov V V, Kukhanova M K, Sal'nikova N E, Nikolaeva L V, Kraevskiĭ A A
Mol Biol (Mosk). 1977 May-Jun;11(3):671-6.
It has been shown that 50S subunits of E. coli MRE-600 ribosomes catalyze the reaction of N-(formyl)-methionyl ester of adenosine 5'-phosphate acting as peptide donor, with Phe-tRNA or CACCA-Phe serving as a peptide acceptor. The reaction is stimulated by cytidine 5'phosphate and inhibited by lincomycin, puromycin and chloramphenicol. The obtained results show that the structure of the donor site of peptidyltransferase is completely assembled on the 50S subunit and 30S subunit is not required for its formation.
已经表明,大肠杆菌MRE - 600核糖体的50S亚基催化5'-磷酸腺苷的N-(甲酰基)-甲硫氨酰酯作为肽供体与苯丙氨酰 - tRNA或CACCA - 苯丙氨酸作为肽受体的反应。该反应受到5'-磷酸胞苷的刺激,并受到林可霉素、嘌呤霉素和氯霉素的抑制。所得结果表明,肽基转移酶供体位点的结构完全在50S亚基上组装完成,其形成不需要30S亚基。