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Updated: Feb 5, 2026

Genome-wide Analysis of Aminoacylation Charging Levels of tRNA Using Microarrays
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RpbL12 Assists Catalysis by Correctly Positioning the Incoming Aminoacyl-tRNA in the A-Site of

Jean-Bernard Créchet1, Fulbert K Agbo'Saga2, Soria Baouz2

  • 1Ecole Polytechnique, Route de Saclay, F-91120 Palaiseau, France.

The Open Biochemistry Journal
|September 11, 2018
PubMed
Summary
This summary is machine-generated.

Lysine-65 in E. coli RpbL12 is crucial for ribosomal function, specifically aiding aminoacyl-tRNA binding to the A-site. Mutations impair activity unless a positive charge is maintained, highlighting its role beyond peptidyl transfer.

Keywords:
Aminoacyl-tRNAE. coli ribosomal protein bL12GGQ-like GAN motif of bL12Lys-65 of bL12Mechanism of peptide bond formationSite-directed mutagenesis

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Area of Science:

  • Molecular Biology
  • Ribosome Function
  • Protein Biochemistry

Background:

  • Previous studies showed Lysine-65 (Lys-65) in the E. coli RpbL12 62GANK65 motif is essential for activity when affinity labeled.
  • This residue is located in a critical region of the ribosomal protein L12.

Purpose of the Study:

  • To investigate the specific role of Lys-65 in ribosomal activity and aminoacyl-tRNA binding.
  • To determine the functional requirements of Lys-65, particularly the necessity of its positive charge.

Main Methods:

  • Site-directed mutagenesis of Lys-65 in E. coli RpbL12.
  • Assessing the activity of mutant ribosomes in protein synthesis.
  • Evaluating the role of Lys-65 in peptidyl transferase activity using puromycin.
  • Analyzing the effect of Lys-65 mutations on aminoacyl-tRNA binding to the ribosomal A-site.

Main Results:

  • Mutations at Lys-65 generally impaired ribosomal activity, except for K65R and K65H mutants, indicating a positive charge is essential.
  • Lys-65 was not involved in the peptidyl transferase reaction with puromycin.
  • Lys-65 facilitates the binding of incoming aminoacyl-tRNA to the ribosomal A-site.

Conclusions:

  • The positive charge of Lys-65 is critical for its function in facilitating aminoacyl-tRNA binding.
  • Lys-65 likely interacts with the phosphate groups of aminoacyl-tRNA via ionic bonds, ensuring proper positioning for peptide bond formation.
  • The unprotonated εNH2 form of Lys-65 may act as a proton acceptor, facilitating the deprotonation of the aminoacyl-tRNA α-amino group.