Inactivation of Ribosomes In Vitro by Colicin E 3 and Its Mechanism of Action
Author(s) -
Thierry Boon
Publication year - 1972
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.69.3.549
Subject(s) - colicin , ribosome , ribosomal rna , cleavage (geology) , protein subunit , biology , escherichia coli , in vitro , 50s , bacteriocin , biochemistry , rna , microbiology and biotechnology , bacteria , genetics , paleontology , fracture (geology) , gene
The incubation of purified ribosomes with colicin E(3) results in the cleavage of a terminal fragment from the 16S ribosomal RNA. The cleavage reaction requires three components: colicin E(3), the 30S ribosomal subunit, and the 50S ribosomal subunit. An immunity factor found in extracts derived from colicinogenic cells prevents the in vitro inactivation of ribosomes by colicin E(3). Evidence is presented suggesting that it does so by binding to the colicin molecule. The mode of action of colicin E(3)in vivo can be explained by the assumption that a small fraction of the adsorbed colicin penetrates into the cell and catalytically inactivates the ribosomes.
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