Tinashe P. Maviza

TL;DR: Structural and biochemical analysis reveal that tetracenomycin X acts as an inhibitor of protein synthesis by binding within the exit tunnel in a large ribosomal unit to prevent the prolongation of the nascent polypeptide chain.

TL;DR: In this article, the authors report the isolation and structure elucidation of a novel natural tetracenomycin X congener, 6-hydroxytetraceonomycin X (6-OH-TcmX), which exhibited lower antimicrobial and cytotoxic activity, but comparable in vitro protein synthesis inhibition ability.

TL;DR: Structural and kinetic analyses reveal that argyrins inhibit protein synthesis by interacting with, and trapping, the translation elongation factor G (EF-G) on the ribosome, analogous to that reported previously for the unrelated antibiotic fusidic acid.

TL;DR: It is observed that in Gram-negative E. coli ΔtolC strain with enhanced permeability, wild-type gyrase and GyrA S83L mutant, resistant to fluoroquinolones, are both similarly sensitive to nybomycin.

TL;DR: It is demonstrated that the viability of E. coli ATCC25922 strain that is devoid of rtcB2 and prfH genes is impaired upon action of colicin E3, in contrast to the parental strain which has intact rTCB 2 and prFH genes.