Structural and functional characterization of the bacterial translocation inhibitor GE82832.

Abstract:

:The structure of GE82832, a translocation inhibitor produced by a soil microorganism, is shown to be highly related to that of dityromycin, a bicyclodecadepsipeptide antibiotic discovered long ago whose characterization had never been pursued beyond its structural elucidation. GE82832 and dityromycin were shown to interfere with both aminoacyl-tRNA and mRNA movement and with the Pi release occurring after ribosome- and EF-G-dependent GTP hydrolysis. These findings and the unusual ribosomal localization of GE82832/dityromycin near protein S13 suggest that the mechanism of inhibition entails an interference with the rotation of the 30S subunit "head" which accompanies the ribosome-unlocking step of translocation.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Brandi L,Maffioli S,Donadio S,Quaglia F,Sette M,Milón P,Gualerzi CO,Fabbretti A

doi

10.1016/j.febslet.2012.07.040

subject

Has Abstract

pub_date

2012-09-21 00:00:00

pages

3373-8

issue

19

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(12)00608-4

journal_volume

586

pub_type

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