期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1972
卷号：69
期号：12
页码：3602-3605
DOI：10.1073/pnas.69.12.3602
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Polypeptide chain initiation factor IF-2 binds to 30S ribosomal subunits. This binding is enhanced by IF-1 and IF-3. During GTP-dependent formation of a 70S initiation complex, IF-2 is released from the ribosome. During 70S initiation complex formation dependent on the methylene analogue of GTP, GMPPCH2P, IF-2 is not released, but remains bound to the 70S ribosome. This result suggests that IF-2 release requires GTP hydrolysis. In agreement with this presumed requirement, IF-2 functions catalytically with GTP, but stoichiometrically with GMPPCH2P, in bringing about 70S initiation complex formation.
