On the interaction of colicin E3 with the ribosome

Raz Zarivach, Efrat Ben-Zeev, Nan Wu, Tamar Auerbach, Anat Bashan, Karen Jakes, Katherine Dickman, Alexander Kosmidis, Frank Schluenzen, Ada Yonath, Miriam Eisenstein, Menachem Shoham

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

Colicin E3 is a protein that kills Escherichia coli cells by a process that involves binding to a surface receptor, entering the cell and inactivating its protein biosynthetic machinery. Colicin E3 kills cells by a catalytic mechanism of a specific ribonucleolytic cleavage in 16S rRNA at the ribosomal decoding A-site between A1493 and G1494 (E. coli numbering system). The breaking of this single phosphodiester bond results in a complete cessation of protein biosynthesis and cell death. The inactive E517Q mutant of the catalytic domain of colicin E3 binds to 30S ribosomal subunits of Thermus thermophilus, as demonstrated by an immunoblotting assay. A model structure of the complex of the ribosomal subunit 30S and colicin E3, obtained via docking, explains the role of the catalytic residues, suggests a catalytic mechanism and provides insight into the specificity of the reaction. Furthermore, the model structure suggests that the inhibitory action of bound immunity is due to charge repulsion of this acidic protein by the negatively charged rRNA backbone.

Original languageEnglish
Pages (from-to)447-454
Number of pages8
JournalBiochimie
Volume84
Issue number5-6
DOIs
StatePublished - 1 May 2002
Externally publishedYes

Keywords

  • Bacteriocin
  • Colicin E3
  • Protein biosynthesis
  • RNase
  • Ribosome
  • Toxin

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