Pyrazinamide triggers degradation of its target aspartate decarboxylase

It has been shown that the bioactive component of pyrazinamide, pyrazinoic acid (POA), blocks coenzyme A biosynthesis in M. tuberculosis by binding to the aspartate decarboxylase PanD. Here the authors show that pyrazinamide triggers degradation of PanD by stimulating its degradation by the caseinol...

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Autores principales:	Pooja Gopal, Jickky Palmae Sarathy, Michelle Yee, Priya Ragunathan, Joon Shin, Shashi Bhushan, Junhao Zhu, Tatos Akopian, Olga Kandror, Teck Kwang Lim, Martin Gengenbacher, Qingsong Lin, Eric J. Rubin, Gerhard Grüber, Thomas Dick
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/840f3d486eeb4f43af457982724b4b9d
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spelling	oai:doaj.org-article:840f3d486eeb4f43af457982724b4b9d2021-12-02T15:39:13ZPyrazinamide triggers degradation of its target aspartate decarboxylase10.1038/s41467-020-15516-12041-1723https://doaj.org/article/840f3d486eeb4f43af457982724b4b9d2020-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-15516-1https://doaj.org/toc/2041-1723It has been shown that the bioactive component of pyrazinamide, pyrazinoic acid (POA), blocks coenzyme A biosynthesis in M. tuberculosis by binding to the aspartate decarboxylase PanD. Here the authors show that pyrazinamide triggers degradation of PanD by stimulating its degradation by the caseinolytic protease Clp.Pooja GopalJickky Palmae SarathyMichelle YeePriya RagunathanJoon ShinShashi BhushanJunhao ZhuTatos AkopianOlga KandrorTeck Kwang LimMartin GengenbacherQingsong LinEric J. RubinGerhard GrüberThomas DickNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Pooja Gopal Jickky Palmae Sarathy Michelle Yee Priya Ragunathan Joon Shin Shashi Bhushan Junhao Zhu Tatos Akopian Olga Kandror Teck Kwang Lim Martin Gengenbacher Qingsong Lin Eric J. Rubin Gerhard Grüber Thomas Dick Pyrazinamide triggers degradation of its target aspartate decarboxylase
description	It has been shown that the bioactive component of pyrazinamide, pyrazinoic acid (POA), blocks coenzyme A biosynthesis in M. tuberculosis by binding to the aspartate decarboxylase PanD. Here the authors show that pyrazinamide triggers degradation of PanD by stimulating its degradation by the caseinolytic protease Clp.
format	article
author	Pooja Gopal Jickky Palmae Sarathy Michelle Yee Priya Ragunathan Joon Shin Shashi Bhushan Junhao Zhu Tatos Akopian Olga Kandror Teck Kwang Lim Martin Gengenbacher Qingsong Lin Eric J. Rubin Gerhard Grüber Thomas Dick
author_facet	Pooja Gopal Jickky Palmae Sarathy Michelle Yee Priya Ragunathan Joon Shin Shashi Bhushan Junhao Zhu Tatos Akopian Olga Kandror Teck Kwang Lim Martin Gengenbacher Qingsong Lin Eric J. Rubin Gerhard Grüber Thomas Dick
author_sort	Pooja Gopal
title	Pyrazinamide triggers degradation of its target aspartate decarboxylase
title_short	Pyrazinamide triggers degradation of its target aspartate decarboxylase
title_full	Pyrazinamide triggers degradation of its target aspartate decarboxylase
title_fullStr	Pyrazinamide triggers degradation of its target aspartate decarboxylase
title_full_unstemmed	Pyrazinamide triggers degradation of its target aspartate decarboxylase
title_sort	pyrazinamide triggers degradation of its target aspartate decarboxylase
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/840f3d486eeb4f43af457982724b4b9d
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Pyrazinamide triggers degradation of its target aspartate decarboxylase

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