期刊论文详细信息
FEBS Letters | |
The interaction of ribosomal protein L16 and its fragments with tRNA | |
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
【 预 览 】
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