VapC toxins from Mycobacterium tuberculosis are ribonucleases that differentially inhibit growth and are neutralized by cognate vapB antitoxins

10.1371/journal.pone.0021738

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Main Authors:	Ahidjo B.A., Kuhnert D., McKenzie J.L., Machowski E.E., Gordhan B.G., Arcus V., Abrahams G.L., Mizrahi V.
Other Authors:	MICROBIOLOGY AND IMMUNOLOGY
Format:	Article
Published:	Public Library of Science 2020
Subjects:	antitoxin bacterial toxin ribonuclease tetracycline unclassified drug vapB toxin vapC toxin bacterial protein article bacterial gene bacterial growth controlled study enzyme activity gene deletion gene expression regulation gene function gene locus gene overexpression genetic selection growth inhibition Mycobacterium smegmatis Mycobacterium tuberculosis nonhuman operon phenotype promoter region protein expression protein function protein protein interaction toxin analysis genetics growth, development and aging metabolism physiology Antitoxins Bacterial Proteins Gene Expression Regulation, Bacterial Ribonucleases
Online Access:	https://scholarbank.nus.edu.sg/handle/10635/165590
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1655902024-11-10T08:17:27Z VapC toxins from Mycobacterium tuberculosis are ribonucleases that differentially inhibit growth and are neutralized by cognate vapB antitoxins Ahidjo B.A. Kuhnert D. McKenzie J.L. Machowski E.E. Gordhan B.G. Arcus V. Abrahams G.L. Mizrahi V. MICROBIOLOGY AND IMMUNOLOGY antitoxin bacterial toxin ribonuclease tetracycline unclassified drug vapB toxin vapC toxin bacterial protein ribonuclease article bacterial gene bacterial growth controlled study enzyme activity gene deletion gene expression regulation gene function gene locus gene overexpression genetic selection growth inhibition Mycobacterium smegmatis Mycobacterium tuberculosis nonhuman operon phenotype promoter region protein expression protein function protein protein interaction toxin analysis genetics growth, development and aging metabolism Mycobacterium tuberculosis physiology Mycobacterium tuberculosis Antitoxins Bacterial Proteins Gene Expression Regulation, Bacterial Mycobacterium tuberculosis Ribonucleases 10.1371/journal.pone.0021738 PLoS ONE 6 6 e21738 2020-03-18T05:49:33Z 2020-03-18T05:49:33Z 2011 Article Ahidjo B.A., Kuhnert D., McKenzie J.L., Machowski E.E., Gordhan B.G., Arcus V., Abrahams G.L., Mizrahi V. (2011). VapC toxins from Mycobacterium tuberculosis are ribonucleases that differentially inhibit growth and are neutralized by cognate vapB antitoxins. PLoS ONE 6 (6) : e21738. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0021738 19326203 https://scholarbank.nus.edu.sg/handle/10635/165590 Public Library of Science Unpaywall 20200320
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	antitoxin bacterial toxin ribonuclease tetracycline unclassified drug vapB toxin vapC toxin bacterial protein ribonuclease article bacterial gene bacterial growth controlled study enzyme activity gene deletion gene expression regulation gene function gene locus gene overexpression genetic selection growth inhibition Mycobacterium smegmatis Mycobacterium tuberculosis nonhuman operon phenotype promoter region protein expression protein function protein protein interaction toxin analysis genetics growth, development and aging metabolism Mycobacterium tuberculosis physiology Mycobacterium tuberculosis Antitoxins Bacterial Proteins Gene Expression Regulation, Bacterial Mycobacterium tuberculosis Ribonucleases
spellingShingle	antitoxin bacterial toxin ribonuclease tetracycline unclassified drug vapB toxin vapC toxin bacterial protein ribonuclease article bacterial gene bacterial growth controlled study enzyme activity gene deletion gene expression regulation gene function gene locus gene overexpression genetic selection growth inhibition Mycobacterium smegmatis Mycobacterium tuberculosis nonhuman operon phenotype promoter region protein expression protein function protein protein interaction toxin analysis genetics growth, development and aging metabolism Mycobacterium tuberculosis physiology Mycobacterium tuberculosis Antitoxins Bacterial Proteins Gene Expression Regulation, Bacterial Mycobacterium tuberculosis Ribonucleases Ahidjo B.A. Kuhnert D. McKenzie J.L. Machowski E.E. Gordhan B.G. Arcus V. Abrahams G.L. Mizrahi V. VapC toxins from Mycobacterium tuberculosis are ribonucleases that differentially inhibit growth and are neutralized by cognate vapB antitoxins
description	10.1371/journal.pone.0021738
author2	MICROBIOLOGY AND IMMUNOLOGY
author_facet	MICROBIOLOGY AND IMMUNOLOGY Ahidjo B.A. Kuhnert D. McKenzie J.L. Machowski E.E. Gordhan B.G. Arcus V. Abrahams G.L. Mizrahi V.
format	Article
author	Ahidjo B.A. Kuhnert D. McKenzie J.L. Machowski E.E. Gordhan B.G. Arcus V. Abrahams G.L. Mizrahi V.
author_sort	Ahidjo B.A.
title	VapC toxins from Mycobacterium tuberculosis are ribonucleases that differentially inhibit growth and are neutralized by cognate vapB antitoxins
title_short	VapC toxins from Mycobacterium tuberculosis are ribonucleases that differentially inhibit growth and are neutralized by cognate vapB antitoxins
title_full	VapC toxins from Mycobacterium tuberculosis are ribonucleases that differentially inhibit growth and are neutralized by cognate vapB antitoxins
title_fullStr	VapC toxins from Mycobacterium tuberculosis are ribonucleases that differentially inhibit growth and are neutralized by cognate vapB antitoxins
title_full_unstemmed	VapC toxins from Mycobacterium tuberculosis are ribonucleases that differentially inhibit growth and are neutralized by cognate vapB antitoxins
title_sort	vapc toxins from mycobacterium tuberculosis are ribonucleases that differentially inhibit growth and are neutralized by cognate vapb antitoxins
publisher	Public Library of Science
publishDate	2020
url	https://scholarbank.nus.edu.sg/handle/10635/165590
_version_	1821232108088066048

VapC toxins from Mycobacterium tuberculosis are ribonucleases that differentially inhibit growth and are neutralized by cognate vapB antitoxins

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