The properties of the complex between ribosomal protein L2 and tRNA.
Escherichia coli ribosomal protein L2 interacts with fMet-tRNAfMet and NacPhe-tRNAPhe in solution, protecting their 3'-ends from enzymatic degradation. At the same time L2 enhances the rate of spontaneous hydrolysis of the ester bonds between terminal riboses and amino acyl moieties of these two peptidyl-tRNA analogues. L2 has, however, only a slight effect on the rate of spontaneous deacylation of aminoacyl-tRNAs. We suggest that the role of L2 is in the fixation of the aminoacyl stem of tRNA to the ribosome at its P-site, and speculate that this protein is directly involved in the peptidyl transferase (PT) reaction.
J
J
Remme
E
E
Metspalu
T
T
Maimets
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R
Villems
D001426:Bacterial Proteins / Q000378:metabolism; D001665:Binding Sites; D004926:Escherichia coli / Q000378:metabolism; D006207:Half-Life; D006868:Hydrolysis; D011485:Protein Binding; D012329:RNA, Bacterial / Q000378:metabolism; D012343:RNA, Transfer / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism*
D001426:Bacterial Proteins; D012329:RNA, Bacterial; D012269:Ribosomal Proteins; C029466:ribosomal protein L2; D012343:RNA, Transfer