Further evidence for the participation of proteins S 3, S 14 and S 19 in tRNA binding toE. coli30 S subunits
✍ Scribed by Marilyn Shimizu; Gary R. Craven
- Publisher
- Springer
- Year
- 1976
- Tongue
- English
- Weight
- 378 KB
- Volume
- 3
- Category
- Article
- ISSN
- 0301-4851
No coin nor oath required. For personal study only.
✦ Synopsis
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.