RNA Therapeutics Institute Publications

Title

Mechanism of Inhibition of Translation Termination by Blasticidin S

UMMS Affiliation

RNA Therapeutics Institute

Publication Date

2018-03-02

Document Type

Article

Disciplines

Biochemistry, Biophysics, and Structural Biology

Abstract

Understanding the mechanisms of inhibitors of translation termination may inform development of new antibacterials and therapeutics for premature termination diseases. We report the crystal structure of the potent termination inhibitor blasticidin S bound to the ribosomal 70S*release factor 1 (RF1) termination complex. Blasticidin S shifts the catalytic domain 3 of RF1 and restructures the peptidyl transferase center. Universally conserved uridine 2585 in the peptidyl transferase center occludes the catalytic backbone of the GGQ motif of RF1, explaining the structural mechanism of inhibition. Rearrangement of domain 3 relative to the codon-recognition domain 2 provides insight into the dynamics of RF1 implicated in termination accuracy.

Keywords

RF1, antibiotic, blasticidin S, stop-codon recognition, termination suppression

DOI of Published Version

10.1016/j.jmb.2018.01.007

Source

J Mol Biol. 2018 Mar 2;430(5):591-593. doi: 10.1016/j.jmb.2018.01.007. Link to article on publisher's site

Journal/Book/Conference Title

Journal of molecular biology

Related Resources

Link to Article in PubMed

PubMed ID

29366636

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