蛋白质S3、S14和S19参与转运核糖核酸与大肠杆菌30S亚基结合的进一步证据。

Further evidence for the participation of proteins S 3, S 14 and S 19 in tRNA binding to E. coli 30 S subunits.

作者信息

Shimizu M, Craven G R

出版信息

Mol Biol Rep. 1976 Nov;3(2):105-11. doi: 10.1007/BF00423223.

Abstract

Previous studies have shown that iodination of 30 S subunits causes inactivation for both enzymatic fMet-tRNA and non-enzymatic phe-tRNA binding activities. This inactivation was shown to be due to the modification of three to five ribosomal proteins [1]. In this report the role of these proteins in tRNA binding activity has been further studied. Purified ribosomal proteins, isolated from modified subunits, are re-assembled into otherwise unmodified 30 S ribosomes and assayed for tRNA binding capacity. The presence of modified S 3, S 14 and S 19 (S 15) in the reconstituted particle results in substantial reduction of both fMet-tRNA and phe-tRNA binding activities. This reduction in tRNA binding activity does not appear to be due to an assembly defect.

摘要

先前的研究表明，30 S亚基的碘化会导致酶促甲硫氨酸- tRNA和非酶促苯丙氨酸- tRNA结合活性失活。这种失活被证明是由于三到五种核糖体蛋白的修饰[1]。在本报告中，进一步研究了这些蛋白质在tRNA结合活性中的作用。从修饰的亚基中分离出的纯化核糖体蛋白，重新组装到其他未修饰的30 S核糖体中，并检测其tRNA结合能力。重组颗粒中存在修饰的S 3、S 14和S 19（S 15）会导致甲硫氨酸- tRNA和苯丙氨酸- tRNA结合活性大幅降低。tRNA结合活性的这种降低似乎不是由于组装缺陷。