Structural and functional characterization of the bacterial translocation inhibitor GE82832

Letizia Brandi; Sonia Maffioli; Stefano Donadio; Fabio Quaglia; Marco Sette; Pohl Milón; Claudio O. Gualerzi; Attilio Fabbretti

doi:10.1016/j.febslet.2012.07.040

Structural and functional characterization of the bacterial translocation inhibitor GE82832

Letizia Brandi, Sonia Maffioli, Stefano Donadio, Fabio Quaglia, Marco Sette, Pohl Milón, Claudio O. Gualerzi, Attilio Fabbretti

Research output: Contribution to journal › Article › peer-review

24 Scopus citations

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.

Original language	English
Pages (from-to)	3373-3378
Number of pages	6
Journal	FEBS Letters
Volume	586
Issue number	19
DOIs	https://doi.org/10.1016/j.febslet.2012.07.040
State	Published - 21 Sep 2012
Externally published	Yes

Keywords

Dityromycin
Natural product
Ribosome
Translation
Translocation inhibitor

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10.1016/j.febslet.2012.07.040

Cite this

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title = "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.",

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T1 - Structural and functional characterization of the bacterial translocation inhibitor GE82832

AU - Brandi, Letizia

AU - Maffioli, Sonia

AU - Donadio, Stefano

AU - Quaglia, Fabio

AU - Sette, Marco

AU - Milón, Pohl

AU - Gualerzi, Claudio O.

AU - Fabbretti, Attilio

PY - 2012/9/21

Y1 - 2012/9/21

N2 - 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.

AB - 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.

KW - Dityromycin

KW - Natural product

KW - Ribosome

KW - Translation

KW - Translocation inhibitor

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DO - 10.1016/j.febslet.2012.07.040

M3 - Artículo

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AN - SCOPUS:84866625243

SN - 0014-5793

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EP - 3378

JO - FEBS Letters

JF - FEBS Letters

IS - 19

ER -

Structural and functional characterization of the bacterial translocation inhibitor GE82832

Abstract

Keywords

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