Cargando…

Error-prone initiation factor 2 mutations reduce the fitness cost of antibiotic resistance

Mutations in the fmt gene (encoding formyl methionine transferase) that eliminate formylation of initiator tRNA (Met-tRNA(i)) confer resistance to the novel antibiotic class of peptide deformylase inhibitors (PDFIs) while concomitantly reducing bacterial fitness. Here we show in Salmonella typhimuri...

Descripción completa

Detalles Bibliográficos
Autores principales:	Zorzet, Anna, Pavlov, Michael Y, Nilsson, Annika I, Ehrenberg, Måns, Andersson, Dan I
Formato:	Texto
Lenguaje:	English
Publicado:	Blackwell Publishing Ltd 2010
Materias:	Research Articles
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2859245/ https://www.ncbi.nlm.nih.gov/pubmed/20132454 http://dx.doi.org/10.1111/j.1365-2958.2010.07057.x

Ejemplares similares

Compensating the Fitness Costs of Synonymous Mutations
por: Knöppel, Anna, et al.
Publicado: (2016)

The mechanism of error induction by the antibiotic viomycin provides insight into the fidelity mechanism of translation
por: Holm, Mikael, et al.
Publicado: (2019)

The fitness costs of antibiotic resistance mutations
por: Melnyk, Anita H, et al.
Publicado: (2015)

Antibiotic Minimal Selective Concentrations and Fitness Costs during Biofilm and Planktonic Growth
por: Hjort, Karin, et al.
Publicado: (2022)

A conformational switch in initiation factor 2 controls the fidelity of translation initiation in bacteria
por: Caban, Kelvin, et al.
Publicado: (2017)

Error-Prone Candidates Vie for Somatic Mutation
por: Poltoratsky, Vladimir, et al.
Publicado: (2000)

Fitness Costs of Synonymous Mutations in the rpsT Gene Can Be Compensated by Restoring mRNA Base Pairing
por: Lind, Peter A., et al.
Publicado: (2013)

Nonmutational compensation of the fitness cost of antibiotic resistance in mycobacteria by overexpression of tlyA rRNA methylase
por: Freihofer, Pietro, et al.
Publicado: (2016)

Error-prone polymerase activity causes multinucleotide mutations in humans
por: Harris, Kelley, et al.
Publicado: (2014)

Ethanol exposure increases mutation rate through error-prone polymerases
por: Voordeckers, Karin, et al.
Publicado: (2020)

Reducing Antibiotic Prescription Errors in the Emergency Department: A Quality Improvement Initiative
por: Kasmire, Kathryn E., et al.
Publicado: (2020)

Proofreading neutralizes potential error hotspots in genetic code translation by transfer RNAs
por: Zhang, Jingji, et al.
Publicado: (2016)

Complete kinetic mechanism for recycling of the bacterial ribosome
por: Borg, Anneli, et al.
Publicado: (2016)

Mechanism of fusidic acid inhibition of RRF- and EF-G-dependent splitting of the bacterial post-termination ribosome
por: Borg, Anneli, et al.
Publicado: (2016)

Fitness of Escherichia coli mutants with reduced susceptibility to tigecycline
por: Linkevicius, Marius, et al.
Publicado: (2016)

The DnaK Chaperone System Buffers the Fitness Cost of Antibiotic Resistance Mutations in Mycobacteria
por: Fay, Allison, et al.
Publicado: (2021)

Accurate and fast methods to estimate the population mutation rate from error prone sequences
por: Knudsen, Bjarne, et al.
Publicado: (2009)

Construction of a highly error-prone DNA polymerase for developing organelle mutation systems
por: Ji, Junwei, et al.
Publicado: (2020)

Accuracy of genetic code translation and its orthogonal corruption by aminoglycosides and Mg(2+) ions
por: Zhang, Jingji, et al.
Publicado: (2018)

A recent intermezzo at the Ribosome Club
por: Pavlov, Michael Y., et al.
Publicado: (2017)

Replicative mechanisms for CNV formation are error prone
por: Carvalho, Claudia M. B., et al.
Publicado: (2013)

Interspecies interaction reduces selection for antibiotic resistance in Escherichia coli
por: Nair, Ramith R., et al.
Publicado: (2023)

Error-prone bypass of DNA lesions during lagging strand replication is a common source of germline and cancer mutations
por: Seplyarskiy, Vladimir B., et al.
Publicado: (2018)

In vitro mutation artifacts after formalin fixation and error prone translesion synthesis during PCR
por: Quach, Nancy, et al.
Publicado: (2004)

Error-prone DNA polymerase and oxidative stress increase the incidences of A to G mutations in tumors
por: Lin, Jiannan, et al.
Publicado: (2016)

Antimicrobial Peptide Exposure Selects for Resistant and Fit Stenotrophomonas maltophilia Mutants That Show Cross-Resistance to Antibiotics
por: Blanco, Paula, et al.
Publicado: (2020)

Dissecting the Fitness Costs of Complex Mutations
por: Yubero, Pablo, et al.
Publicado: (2021)

Predictable Phenotypes of Antibiotic Resistance Mutations
por: Knopp, M., et al.
Publicado: (2018)

Fitness Costs of Mutations at the HIV-1 Capsid Hexamerization Interface
por: Manocheewa, Siriphan, et al.
Publicado: (2013)

Size and Shape Analysis of Error-Prone Shape Data
por: Du, Jiejun, et al.
Publicado: (2015)

Premature aging in mice with error-prone protein synthesis
por: Shcherbakov, Dimitri, et al.
Publicado: (2022)

Seed biologists beware: Estimates of initial viability based on ungerminated seeds at the end of an experiment may be error‐prone
por: Lamont, B. B.
Publicado: (2022)

Ribosome formation from subunits studied by stopped-flow and Rayleigh light scattering
por: Antoun, Ayman, et al.
Publicado: (2004)

Estimation of peptide elongation times from ribosome profiling spectra
por: Pavlov, Michael Y, et al.
Publicado: (2021)

Structural Bases for the Fitness Cost of the Antibiotic-Resistance and Lethal Mutations at Position 1408 of 16S rRNA
por: Kondo, Jiro, et al.
Publicado: (2019)

Compensatory mutations reducing the fitness cost of plasmid carriage occur in plant rhizosphere communities
por: Bird, Susannah M, et al.
Publicado: (2023)

Error-prone DnaE2 Balances the Genome Mutation Rates in Myxococcus xanthus DK1622
por: Peng, Ran, et al.
Publicado: (2017)

Mechanisms and Fitness Costs of Resistance to Antimicrobial Peptides LL-37, CNY100HL and Wheat Germ Histones
por: Lofton, Hava, et al.
Publicado: (2013)

A comparative evaluation of hybrid error correction methods for error-prone long reads
por: Fu, Shuhua, et al.
Publicado: (2019)

Guanine-nucleotide exchange on ribosome-bound elongation factor G initiates the translocation of tRNAs
por: Zavialov, Andrey V, et al.
Publicado: (2005)

Cannot write session to /tmp/vufind_sessions/sess_hr23banaffbfqs9fki0cep6327