A Conserved Mitochondrial Chaperone-Protease Complex Involved in Protein Homeostasis

Mitochondria are essential organelles involved in cellular energy production. The inner mitochondrial membrane protein stomatin-like protein 2 (SLP-2) is a member of the SPFH (stomatin, prohibitin, flotilin, and HflK/C) superfamily and binds to the mitochondrial glycerophospholipid cardiolipin, form...

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Autores principales:	Mauro Serricchio, Peter Bütikofer
Formato:	article
Lenguaje:	EN
Publicado:	Frontiers Media S.A. 2021
Materias:	cardiolipin stomatin-like protein 2 Yme1 prohibitin mitochondria mitochondrial stress response Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/6c4f41a3f2da49f5a5077803dab77de8
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spelling	oai:doaj.org-article:6c4f41a3f2da49f5a5077803dab77de82021-11-09T05:27:54ZA Conserved Mitochondrial Chaperone-Protease Complex Involved in Protein Homeostasis2296-889X10.3389/fmolb.2021.767088https://doaj.org/article/6c4f41a3f2da49f5a5077803dab77de82021-11-01T00:00:00Zhttps://www.frontiersin.org/articles/10.3389/fmolb.2021.767088/fullhttps://doaj.org/toc/2296-889XMitochondria are essential organelles involved in cellular energy production. The inner mitochondrial membrane protein stomatin-like protein 2 (SLP-2) is a member of the SPFH (stomatin, prohibitin, flotilin, and HflK/C) superfamily and binds to the mitochondrial glycerophospholipid cardiolipin, forming cardiolipin-enriched membrane domains to promote the assembly and/or stabilization of protein complexes involved in oxidative phosphorylation. In addition, human SLP-2 anchors a mitochondrial processing complex required for proteolytic regulation of proteins involved in mitochondrial dynamics and quality control. We now show that deletion of the gene encoding the Trypanosoma brucei homolog TbSlp2 has no effect on respiratory protein complex stability and mitochondrial functions under normal culture conditions and is dispensable for growth of T. brucei parasites. In addition, we demonstrate that TbSlp2 binds to the metalloprotease TbYme1 and together they form a large mitochondrial protein complex. The two proteins negatively regulate each other’s expression levels by accelerating protein turnover. Furthermore, we show that TbYme1 plays a role in heat-stress resistance, as TbYme1 knock-out parasites displayed mitochondrial fragmentation and loss of viability when cultured at elevated temperatures. Unbiased interaction studies uncovered putative TbYme1 substrates, some of which were differentially affected by the absence of TbYme1. Our results support emerging evidence for the presence of mitochondrial quality control pathways in this ancient eukaryote.Mauro SerricchioPeter BütikoferFrontiers Media S.A.articlecardiolipinstomatin-like protein 2Yme1prohibitinmitochondriamitochondrial stress responseBiology (General)QH301-705.5ENFrontiers in Molecular Biosciences, Vol 8 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	cardiolipin stomatin-like protein 2 Yme1 prohibitin mitochondria mitochondrial stress response Biology (General) QH301-705.5
spellingShingle	cardiolipin stomatin-like protein 2 Yme1 prohibitin mitochondria mitochondrial stress response Biology (General) QH301-705.5 Mauro Serricchio Peter Bütikofer A Conserved Mitochondrial Chaperone-Protease Complex Involved in Protein Homeostasis
description	Mitochondria are essential organelles involved in cellular energy production. The inner mitochondrial membrane protein stomatin-like protein 2 (SLP-2) is a member of the SPFH (stomatin, prohibitin, flotilin, and HflK/C) superfamily and binds to the mitochondrial glycerophospholipid cardiolipin, forming cardiolipin-enriched membrane domains to promote the assembly and/or stabilization of protein complexes involved in oxidative phosphorylation. In addition, human SLP-2 anchors a mitochondrial processing complex required for proteolytic regulation of proteins involved in mitochondrial dynamics and quality control. We now show that deletion of the gene encoding the Trypanosoma brucei homolog TbSlp2 has no effect on respiratory protein complex stability and mitochondrial functions under normal culture conditions and is dispensable for growth of T. brucei parasites. In addition, we demonstrate that TbSlp2 binds to the metalloprotease TbYme1 and together they form a large mitochondrial protein complex. The two proteins negatively regulate each other’s expression levels by accelerating protein turnover. Furthermore, we show that TbYme1 plays a role in heat-stress resistance, as TbYme1 knock-out parasites displayed mitochondrial fragmentation and loss of viability when cultured at elevated temperatures. Unbiased interaction studies uncovered putative TbYme1 substrates, some of which were differentially affected by the absence of TbYme1. Our results support emerging evidence for the presence of mitochondrial quality control pathways in this ancient eukaryote.
format	article
author	Mauro Serricchio Peter Bütikofer
author_facet	Mauro Serricchio Peter Bütikofer
author_sort	Mauro Serricchio
title	A Conserved Mitochondrial Chaperone-Protease Complex Involved in Protein Homeostasis
title_short	A Conserved Mitochondrial Chaperone-Protease Complex Involved in Protein Homeostasis
title_full	A Conserved Mitochondrial Chaperone-Protease Complex Involved in Protein Homeostasis
title_fullStr	A Conserved Mitochondrial Chaperone-Protease Complex Involved in Protein Homeostasis
title_full_unstemmed	A Conserved Mitochondrial Chaperone-Protease Complex Involved in Protein Homeostasis
title_sort	conserved mitochondrial chaperone-protease complex involved in protein homeostasis
publisher	Frontiers Media S.A.
publishDate	2021
url	https://doaj.org/article/6c4f41a3f2da49f5a5077803dab77de8
work_keys_str_mv	AT mauroserricchio aconservedmitochondrialchaperoneproteasecomplexinvolvedinproteinhomeostasis AT peterbutikofer aconservedmitochondrialchaperoneproteasecomplexinvolvedinproteinhomeostasis AT mauroserricchio conservedmitochondrialchaperoneproteasecomplexinvolvedinproteinhomeostasis AT peterbutikofer conservedmitochondrialchaperoneproteasecomplexinvolvedinproteinhomeostasis
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A Conserved Mitochondrial Chaperone-Protease Complex Involved in Protein Homeostasis

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