Molecular Biology Reports

, Volume 3, Issue 2, pp 105–111 | Cite as

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

  • Marilyn Shimizu
  • Gary R. Craven
Article

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.

Keywords

Ribosomal Protein Binding Activity Binding Capacity Substantial Reduction Assembly Defect 

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Copyright information

© D. Reidel Publishing Company 1976

Authors and Affiliations

  • Marilyn Shimizu
    • 1
    • 2
  • Gary R. Craven
    • 1
    • 2
  1. 1.The Laboratory of Molecular BiologyThe University of WisconsinMadisonUSA
  2. 2.the Department of GeneticsThe University of WisconsinMadisonUSA

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