Histidine-Triad Hydrolases Provide Resistance to Peptide-Nucleotide Antibiotics-Reference-Cited by-同舟云学术

Histidine-Triad Hydrolases Provide Resistance to Peptide-Nucleotide Antibiotics

Published:2020-04-28 Issue:2 Volume:11 Page:
ISSN:2161-2129
Container-title:mBio
language:en
Short-container-title:mBio

Author:

Yagmurov Eldar¹,Tsibulskaya Darya¹²,Livenskyi Alexey²³,Serebryakova Marina²⁴,Wolf Yury I.⁵^ORCID,Borukhov Sergei⁶,Severinov Konstantin¹⁷⁸,Dubiley Svetlana¹²

Affiliation:

1. Center for Life Sciences, Skolkovo Institute of Science and Technology, Skolkovo, Russia

2. Institute of Gene Biology, Russian Academy of Science, Moscow, Russia

3. Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russia

4. A.N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia

5. National Center for Biotechnology Information, National Library of Medicine, Bethesda, Maryland, USA

6. Department of Cell Biology and Neuroscience, Rowan University School of Osteopathic Medicine, Stratford, New Jersey, USA

7. Center for Precision Genome Editing and Genetic Technologies for Biomedicine, Institute of Gene Biology, Russian Academy of Sciences, Moscow, Russia

8. Waksman Institute for Microbiology, Piscataway, New Jersey, USA

Abstract

Uncovering the mechanisms of resistance is a required step for countering the looming antibiotic resistance crisis. In this communication, we show how universally conserved histidine-triad hydrolases provide resistance to microcin C, a potent inhibitor of bacterial protein synthesis.

Funder

HHS | NIH | National Institute of Allergy and Infectious Diseases

Publisher

American Society for Microbiology

Subject

Virology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/mBio.00497-20

Reference37 articles.

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2. Chemical Structure and Translation Inhibition Studies of the Antibiotic Microcin C7

3. Maturation of an Escherichia coli Ribosomal Peptide Antibiotic by ATP-Consuming N−P Bond Formation in Microcin C7

4. The Molecular Mechanism of Aminopropylation of Peptide-Nucleotide Antibiotic Microcin C

5. Microcin C: biosynthesis and mechanisms of bacterial resistance

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