Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition
Abstract
Here, with bacterial resistance becoming a serious threat to global public health, antimicrobial peptides (AMPs) have become a promising area of focus in antibiotic research. AMPs are derived from a diverse range of species, from prokaryotes to humans, with a mechanism of action that often involves disruption of the bacterial cell membrane. Proline-rich antimicrobial peptides (PrAMPs) are instead actively transported inside the bacterial cell where they bind and inactivate specific targets. Recently, it was reported that some PrAMPs, such as Bac71–35, oncocins and apidaecins, bind and inactivate the bacterial ribosome. Here we report the crystal structures of Bac71–35, Pyrrhocoricin, Metalnikowin and two oncocin derivatives, bound to the Thermus thermophilus 70S ribosome. Each of the PrAMPs blocks the peptide exit tunnel of the ribosome by simultaneously occupying three well characterized antibioticbinding sites and interferes with the initiation step of translation, thereby revealing a common mechanism of action used by these PrAMPs to inactivate protein synthesis. Our study expands the repertoire of PrAMPs and provides a framework for designing new-generation therapeutics.
- Authors:
-
- Yale Univ., New Haven, CT (United States)
- Univ. of Illinois at Chicago, Chicago, IL (United States)
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC)
- OSTI Identifier:
- 1243124
- Grant/Contract Number:
- AC02-06CH11357
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nucleic Acids Research (Online)
- Additional Journal Information:
- Journal Name: Nucleic Acids Research (Online); Journal Volume: 44; Journal Issue: 5; Journal ID: ISSN 1362-4962
- Publisher:
- Oxford University Press
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES
Citation Formats
Gagnon, Matthieu G., Roy, Raktim N., Lomakin, Ivan B., Florin, Tanja, Mankin, Alexander S., and Steitz, Thomas A. Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition. United States: N. p., 2016.
Web. doi:10.1093/nar/gkw018.
Gagnon, Matthieu G., Roy, Raktim N., Lomakin, Ivan B., Florin, Tanja, Mankin, Alexander S., & Steitz, Thomas A. Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition. United States. https://doi.org/10.1093/nar/gkw018
Gagnon, Matthieu G., Roy, Raktim N., Lomakin, Ivan B., Florin, Tanja, Mankin, Alexander S., and Steitz, Thomas A. Sun .
"Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition". United States. https://doi.org/10.1093/nar/gkw018. https://www.osti.gov/servlets/purl/1243124.
@article{osti_1243124,
title = {Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition},
author = {Gagnon, Matthieu G. and Roy, Raktim N. and Lomakin, Ivan B. and Florin, Tanja and Mankin, Alexander S. and Steitz, Thomas A.},
abstractNote = {Here, with bacterial resistance becoming a serious threat to global public health, antimicrobial peptides (AMPs) have become a promising area of focus in antibiotic research. AMPs are derived from a diverse range of species, from prokaryotes to humans, with a mechanism of action that often involves disruption of the bacterial cell membrane. Proline-rich antimicrobial peptides (PrAMPs) are instead actively transported inside the bacterial cell where they bind and inactivate specific targets. Recently, it was reported that some PrAMPs, such as Bac71–35, oncocins and apidaecins, bind and inactivate the bacterial ribosome. Here we report the crystal structures of Bac71–35, Pyrrhocoricin, Metalnikowin and two oncocin derivatives, bound to the Thermus thermophilus 70S ribosome. Each of the PrAMPs blocks the peptide exit tunnel of the ribosome by simultaneously occupying three well characterized antibioticbinding sites and interferes with the initiation step of translation, thereby revealing a common mechanism of action used by these PrAMPs to inactivate protein synthesis. Our study expands the repertoire of PrAMPs and provides a framework for designing new-generation therapeutics.},
doi = {10.1093/nar/gkw018},
journal = {Nucleic Acids Research (Online)},
number = 5,
volume = 44,
place = {United States},
year = {Sun Jan 24 00:00:00 EST 2016},
month = {Sun Jan 24 00:00:00 EST 2016}
}
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