The twin-arginine translocation pathway of Mycobacterium smegmatis is functional and required for the export of mycobacterial beta-lactamases. - Wikidata - wikimedia - TriplyDB

The twin-arginine translocation pathway of Mycobacterium smegmatis is functional and required for the export of mycobacterial beta-lactamases.

The twin-arginine translocation pathway of Mycobacterium smegmatis is functional and required for the export of mycobacterial beta-lactamases.

http://www.wikidata.org/entity/Q34124354

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Directed evolution of Mycobacterium tuberculosis β-lactamase reveals gatekeeper residue that regulates antibiotic resistance and catalytic efficiency The twin-arginine translocation pathway in α-proteobacteria is functionally preserved irrespective of genomic and regulatory divergence Characterization of the proteasome accessory factor (paf) operon in Mycobacterium tuberculosis Mycobacterium tuberculosis Cpn60.2 and DnaK are located on the bacterial surface, where Cpn60.2 facilitates efficient bacterial association with macrophages Identification of functional Tat signal sequences in Mycobacterium tuberculosis proteins Inactivation of Rv2525c, a substrate of the twin arginine translocation (Tat) system of Mycobacterium tuberculosis, increases beta-lactam susceptibility and virulence Rv0132c of Mycobacterium tuberculosis encodes a coenzyme F420-dependent hydroxymycolic acid dehydrogenase High Throughput Screen for Escherichia coli Twin Arginine Translocation (Tat) Inhibitors.Genetic toggling of alkaline phosphatase folding reveals signal peptides for all major modes of transport across the inner membrane of bacteria.The PhoP-dependent ncRNA Mcr7 modulates the TAT secretion system in Mycobacterium tuberculosis.LocateP: genome-scale subcellular-location predictor for bacterial proteins.Global transcriptional analysis of spontaneous sakacin P-resistant mutant strains of Listeria monocytogenes during growth on different sugars.Abrogation of the twin arginine transport system in Salmonella enterica serovar Typhimurium leads to colonization defects during infection.Identification and evaluation of twin-arginine translocase inhibitors Rhomboids of Mycobacteria: characterization using an aarA mutant of Providencia stuartii and gene deletion in Mycobacterium smegmatis Tat-dependent translocation of an F420-binding protein of Mycobacterium tuberculosis.Bacterial growth and cell division: a mycobacterial perspective.Mislocalization of Rieske protein PetA predominantly accounts for the aerobic growth defect of Tat mutants in Shewanella oneidensis.Moraxella catarrhalis uses a twin-arginine translocation system to secrete the β-lactamase BRO-2.The rv1184c locus encodes Chp2, an acyltransferase in Mycobacterium tuberculosis polyacyltrehalose lipid biosynthesis.Lipoproteins of slow-growing Mycobacteria carry three fatty acids and are N-acylated by apolipoprotein N-acyltransferase BCG_2070c Molecular Investigations of PenA-mediated β-lactam Resistance in Burkholderia pseudomallei Secretome of obligate intracellular Rickettsia.Copper in microbial pathogenesis: meddling with the metal.Silencing Mycobacterium smegmatis by using tetracycline repressors.Mycobacterial tlyA gene product is localized to the cell-wall without signal sequence.Functional analyses of mycobacterial lipoprotein diacylglyceryl transferase and comparative secretome analysis of a mycobacterial lgt mutant.Mycobacterium marinum Degrades Both Triacylglycerols and Phospholipids from Its Dictyostelium Host to Synthesise Its Own Triacylglycerols and Generate Lipid Inclusions The bacterial twin-arginine translocation pathway.Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain.Protein secretion systems in Mycobacteria.Role of porins for uptake of antibiotics by Mycobacterium smegmatis.Beta-lactamase can function as a reporter of bacterial protein export during Mycobacterium tuberculosis infection of host cells Paradoxical Hypersusceptibility of Drug-resistant Mycobacteriumtuberculosis to β-lactam Antibiotics.Role of the twin-arginine translocation pathway in Staphylococcus.Genomic characterization of Nontuberculous Mycobacteria.Protein export systems of Mycobacterium tuberculosis: novel targets for drug development?The ins and outs of Mycobacterium tuberculosis protein export.The iron-regulated staphylococcal lipoproteins.Mycobacterium tuberculosis evolutionary pathogenesis and its putative impact on drug development.

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The twin-arginine translocation pathway of Mycobacterium smegmatis is functional and required for the export of mycobacterial beta-lactamases.

http://www.wikidata.org/entity/Q34124354

description

2005 nî lūn-bûn

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2005 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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The twin-arginine translocatio ...... mycobacterial beta-lactamases.

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JB.187.22.7667-7679.2005

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Journal of Bacteriology

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The twin-arginine translocatio ...... mycobacterial beta-lactamases.

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P2093

Anthony R Flores

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Justin A McDonough

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Kari E Hacker

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Martin S Pavelka

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Miriam Braunstein

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P2860

Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence

Overlapping functions of components of a bacterial Sec-independent protein export pathway

Novel method for detection of beta-lactamases by using a chromogenic cephalosporin substrate

Recombinant bacillus calmette-guerin (BCG) vaccines expressing the Mycobacterium tuberculosis 30-kDa major secretory protein induce greater protective immunity against tuberculosis than conventional BCG vaccines in a highly susceptible animal model

Improved prediction of signal peptides: SignalP 3.0

Genes required for mycobacterial growth defined by high density mutagenesis

A common export pathway for proteins binding complex redox cofactors?

Consensus statement. Global burden of tuberculosis: estimated incidence, prevalence, and mortality by country. WHO Global Surveillance and Monitoring Project

Topology determination and functional analysis of the Escherichia coli TatC protein

Involvement of the twin-arginine translocation system in protein secretion via the type II pathway

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10.1128/JB.187.22.7667-7679.2005

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1280313

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