The interaction of ribosomal protein L16 and its fragments with tRNA

FEBS Letters

Remme, Jaanus¹  Ustav, Mart²  Villems, Richard¹  Maimets, Toivo² 

[1] Laboratory of Molecular Genetics, Institute of Chemical Physics and Biophysics, 14/16 Kingissepa Str., 202400 Tartu, Estonian SSR, USSR;Laboratory of Molecular Biology, Tartu State University, 202400 Tartu, Estonian SSR, USSR

关键词: Protein L16;    tRNA;    RNA—protein interaction;   

DOI  :  10.1016/0014-5793(83)80621-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Two large proteolytic fragments of Escherichia coli 50 S ribosomal subunit protein L16 were generated by limited hydrolysis with chymotrypsin (missing 9 N-terminal amino acids) and trypsin (missing 16 N-terminal amino acids). It was found that while intact L16 and its chymotryptic fragment both interact with tRNA (K _d = 5.4 x 10⁻⁷ M), the tryptic fragment does not. These results are interpreted in terms of possible significance of the residues 10–16 in the peptidyl transferase activity.

【 授权许可】

Unknown