Ribosomal proteins S12 and S13 function as control elements for translocation of the mRNA:tRNA complex

被引:94
作者
Cukras, AR
Southworth, DR
Brunelle, JL
Culver, GM
Green, R [1 ]
机构
[1] Johns Hopkins Univ, Sch Med, Howard Hughes Med Inst, Dept Mol Biol & Genet, Baltimore, MD 21205 USA
[2] Iowa State Univ Sci & Technol, Dept Biochem Biophys & Mol Biol, Ames, IA 50011 USA
关键词
NON-ENZYMATIC TRANSLOCATION; ELONGATION-FACTOR-G; AMINOACYL-TRANSFER-RNA; ESCHERICHIA-COLI; PARA-CHLOROMERCURIBENZOATE; ANGSTROM RESOLUTION; EF-G; SUBUNIT; SUBPARTICLE; STIMULATION;
D O I
10.1016/S1097-2765(03)00275-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Translocation of the mRNA:tRNA complex through the ribosome is promoted by elongation factor G (EF-G) during the translation cycle. Previous studies established that modification of ribosomal proteins with thiol-specific reagents promotes this event in the absence of EF-G. Here we identify two small subunit interface proteins S12 and S13 that are essential for maintenance of a pretranslocation state. Omission of these proteins using in vitro reconstitution procedures yields ribosomal particles that translate in the absence of enzymatic factors. Conversely, replacement of cysteine residues in these two proteins yields ribosomal particles that are refractive to stimulation with thiol-modifying reagents. These data support a model where S12 and S13 function as control elements for the more ancient rRNA- and tRNA-driven movements of translocation.
引用
收藏
页码:321 / 328
页数:8
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