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The properties of the complex between ribosomal protein L2 and tRNA
Author(s) -
Remme Jaanus,
Metspalu Ene,
Maimets Toivo,
Villems Richard
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81299-0
Subject(s) - transfer rna , ribosomal rna , chemistry , ribosomal protein , ribosome , biochemistry , rna , gene
Escherichia coli ribosomal protein L2 interacts with fMet‐tRNA Met and NacPhe‐tRNA Phe 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 aminoacyltRNAs. 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. Peptidyl transferase Protein L2 tRNA‐protein complex