Mycobacterium tuberculosis ClpP proteases are co-transcribed but exhibit different substrate specificities.

Caseinolytic (Clp) proteases are widespread energy-dependent proteases; the functional ATP-dependent protease is comprised of multimers of proteolytic and regulatory subunits. Mycobacterium tuberculosis has two ClpP proteolytic subunits (ClpP1 and ClpP2), with both being essential for growth in vitr...

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Autores principales:	Yoann Personne, Amanda C Brown, Dorothée L Schuessler, Tanya Parish
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/fb88543b5e7d478ea129b1e11c72688b
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spelling	oai:doaj.org-article:fb88543b5e7d478ea129b1e11c72688b2021-11-18T07:51:12ZMycobacterium tuberculosis ClpP proteases are co-transcribed but exhibit different substrate specificities.1932-620310.1371/journal.pone.0060228https://doaj.org/article/fb88543b5e7d478ea129b1e11c72688b2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23560081/?tool=EBIhttps://doaj.org/toc/1932-6203Caseinolytic (Clp) proteases are widespread energy-dependent proteases; the functional ATP-dependent protease is comprised of multimers of proteolytic and regulatory subunits. Mycobacterium tuberculosis has two ClpP proteolytic subunits (ClpP1 and ClpP2), with both being essential for growth in vitro. ClpP1 and clpP2 are arranged in an apparent operon; we demonstrated that the two genes are co-expressed under normal growth conditions. We identified a single promoter region for the clpP1P2 operon; no promoter was detected upstream of clpP2 demonstrating that independent expression of clpP1 and clpP2 was highly unlikely. Promoter activity was not induced by heat shock or oxidative stress. We identified a regulatory region upstream of the promoter with a consensus sequence matching the ClgR regulator motif; we determined the limits of the region by mutagenesis and confirmed that positive regulation of the promoter occurs in M. tuberculosis. We developed a reporter system to monitor ClpP1 and ClpP2 enzymatic activities based on LacZ incorporating ssrAtag sequences. We showed that whilst both ClpP1 and ClpP2 degrade SsrA-tagged LacZ, ClpP2 (but not ClpP1) degrades untagged proteins. Our data suggest that the two proteolytic subunits display different substrate specificities and therefore have different, but overlapping roles in M. tuberculosis.Yoann PersonneAmanda C BrownDorothée L SchuesslerTanya ParishPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 4, p e60228 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Yoann Personne Amanda C Brown Dorothée L Schuessler Tanya Parish Mycobacterium tuberculosis ClpP proteases are co-transcribed but exhibit different substrate specificities.
description	Caseinolytic (Clp) proteases are widespread energy-dependent proteases; the functional ATP-dependent protease is comprised of multimers of proteolytic and regulatory subunits. Mycobacterium tuberculosis has two ClpP proteolytic subunits (ClpP1 and ClpP2), with both being essential for growth in vitro. ClpP1 and clpP2 are arranged in an apparent operon; we demonstrated that the two genes are co-expressed under normal growth conditions. We identified a single promoter region for the clpP1P2 operon; no promoter was detected upstream of clpP2 demonstrating that independent expression of clpP1 and clpP2 was highly unlikely. Promoter activity was not induced by heat shock or oxidative stress. We identified a regulatory region upstream of the promoter with a consensus sequence matching the ClgR regulator motif; we determined the limits of the region by mutagenesis and confirmed that positive regulation of the promoter occurs in M. tuberculosis. We developed a reporter system to monitor ClpP1 and ClpP2 enzymatic activities based on LacZ incorporating ssrAtag sequences. We showed that whilst both ClpP1 and ClpP2 degrade SsrA-tagged LacZ, ClpP2 (but not ClpP1) degrades untagged proteins. Our data suggest that the two proteolytic subunits display different substrate specificities and therefore have different, but overlapping roles in M. tuberculosis.
format	article
author	Yoann Personne Amanda C Brown Dorothée L Schuessler Tanya Parish
author_facet	Yoann Personne Amanda C Brown Dorothée L Schuessler Tanya Parish
author_sort	Yoann Personne
title	Mycobacterium tuberculosis ClpP proteases are co-transcribed but exhibit different substrate specificities.
title_short	Mycobacterium tuberculosis ClpP proteases are co-transcribed but exhibit different substrate specificities.
title_full	Mycobacterium tuberculosis ClpP proteases are co-transcribed but exhibit different substrate specificities.
title_fullStr	Mycobacterium tuberculosis ClpP proteases are co-transcribed but exhibit different substrate specificities.
title_full_unstemmed	Mycobacterium tuberculosis ClpP proteases are co-transcribed but exhibit different substrate specificities.
title_sort	mycobacterium tuberculosis clpp proteases are co-transcribed but exhibit different substrate specificities.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/fb88543b5e7d478ea129b1e11c72688b
work_keys_str_mv	AT yoannpersonne mycobacteriumtuberculosisclppproteasesarecotranscribedbutexhibitdifferentsubstratespecificities AT amandacbrown mycobacteriumtuberculosisclppproteasesarecotranscribedbutexhibitdifferentsubstratespecificities AT dorotheelschuessler mycobacteriumtuberculosisclppproteasesarecotranscribedbutexhibitdifferentsubstratespecificities AT tanyaparish mycobacteriumtuberculosisclppproteasesarecotranscribedbutexhibitdifferentsubstratespecificities
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Mycobacterium tuberculosis ClpP proteases are co-transcribed but exhibit different substrate specificities.

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