文章基本信息

标题：Met-tRNAfMet Binding to 40S Ribosomal Subunits: A Site for the Regulation of Initiation of Protein Synthesis by Hemin
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作者：Michael J. Clemens ; Edgar C. Henshaw ; Hannah Rahamimoff 等
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：1974
卷号：71
期号：8
页码：2946-2950
DOI：10.1073/pnas.71.8.2946
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：On incubation of reticulocyte lysates at 30{degrees} in the absence of added hemin, protein synthesis declines sharply within 4-6 min, due to the action of a translational inhibitor. Partially purified preparations of this inhibitor, in concentrations that inhibit protein synthesis in the lysate, cause reduced binding of Met-tRNAfMet to derived 40S ribosomal subunits in a ribosomal-salt-wash-dependent assay system. Neither the association of salt wash proteins with the subunits nor the level of Met-tRNAfMet bound in preformed 40S complexes is reduced by the inhibitor. No Met-tRNAfMet deacylase activity could be detected in the inhibitor preparation. Protein synthesis in reticulocyte lysates lacking added hemin or containing exogenous inhibitor is maintained by addition of small amounts of an initiation preparation factor, "F-MP," which may be involved in the binding of Met-tRNAfMet to 40S subunits. This binding constitutes a site for control of protein synthesis by hemin in reticulocytes.
关键词：translation control ; initiation factors ; buoyant density gradients