The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes

Abstract Mitochondrial nucleoids consist of several different groups of proteins, many of which are involved in essential cellular processes such as the replication, repair and transcription of the mitochondrial genome. The eukaryotic, ATP-dependent protease Lon is found within the central nucleoid...

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Autores principales:	Nina Kunová, Gabriela Ondrovičová, Jacob A. Bauer, Jana Bellová, Ľuboš Ambro, Lucia Martináková, Veronika Kotrasová, Eva Kutejová, Vladimír Pevala
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/43baad6c0f9b437c9592997f1f8f7619
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spelling	oai:doaj.org-article:43baad6c0f9b437c9592997f1f8f76192021-12-02T16:07:59ZThe role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes10.1038/s41598-017-00632-82045-2322https://doaj.org/article/43baad6c0f9b437c9592997f1f8f76192017-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-00632-8https://doaj.org/toc/2045-2322Abstract Mitochondrial nucleoids consist of several different groups of proteins, many of which are involved in essential cellular processes such as the replication, repair and transcription of the mitochondrial genome. The eukaryotic, ATP-dependent protease Lon is found within the central nucleoid region, though little is presently known about its role there. Aside from its association with mitochondrial nucleoids, human Lon also specifically interacts with RNA. Recently, Lon was shown to regulate TFAM, the most abundant mtDNA structural factor in human mitochondria. To determine whether Lon also regulates other mitochondrial nucleoid- or ribosome-associated proteins, we examined the in vitro digestion profiles of the Saccharomyces cerevisiae TFAM functional homologue Abf2, the yeast mtDNA maintenance protein Mgm101, and two human mitochondrial proteins, Twinkle helicase and the large ribosomal subunit protein MrpL32. Degradation of Mgm101 was also verified in vivo in yeast mitochondria. These experiments revealed that all four proteins are actively degraded by Lon, but that three of them are protected from it when bound to a nucleic acid; the Twinkle helicase is not. Such a regulatory mechanism might facilitate dynamic changes to the mitochondrial nucleoid, which are crucial for conducting mitochondrial functions and maintaining mitochondrial homeostasis.Nina KunováGabriela OndrovičováJacob A. BauerJana BellováĽuboš AmbroLucia MartinákováVeronika KotrasováEva KutejováVladimír PevalaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Nina Kunová Gabriela Ondrovičová Jacob A. Bauer Jana Bellová Ľuboš Ambro Lucia Martináková Veronika Kotrasová Eva Kutejová Vladimír Pevala The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes
description	Abstract Mitochondrial nucleoids consist of several different groups of proteins, many of which are involved in essential cellular processes such as the replication, repair and transcription of the mitochondrial genome. The eukaryotic, ATP-dependent protease Lon is found within the central nucleoid region, though little is presently known about its role there. Aside from its association with mitochondrial nucleoids, human Lon also specifically interacts with RNA. Recently, Lon was shown to regulate TFAM, the most abundant mtDNA structural factor in human mitochondria. To determine whether Lon also regulates other mitochondrial nucleoid- or ribosome-associated proteins, we examined the in vitro digestion profiles of the Saccharomyces cerevisiae TFAM functional homologue Abf2, the yeast mtDNA maintenance protein Mgm101, and two human mitochondrial proteins, Twinkle helicase and the large ribosomal subunit protein MrpL32. Degradation of Mgm101 was also verified in vivo in yeast mitochondria. These experiments revealed that all four proteins are actively degraded by Lon, but that three of them are protected from it when bound to a nucleic acid; the Twinkle helicase is not. Such a regulatory mechanism might facilitate dynamic changes to the mitochondrial nucleoid, which are crucial for conducting mitochondrial functions and maintaining mitochondrial homeostasis.
format	article
author	Nina Kunová Gabriela Ondrovičová Jacob A. Bauer Jana Bellová Ľuboš Ambro Lucia Martináková Veronika Kotrasová Eva Kutejová Vladimír Pevala
author_facet	Nina Kunová Gabriela Ondrovičová Jacob A. Bauer Jana Bellová Ľuboš Ambro Lucia Martináková Veronika Kotrasová Eva Kutejová Vladimír Pevala
author_sort	Nina Kunová
title	The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes
title_short	The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes
title_full	The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes
title_fullStr	The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes
title_full_unstemmed	The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes
title_sort	role of lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/43baad6c0f9b437c9592997f1f8f7619
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The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes

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