Biological Roles of the Podospora anserina Mitochondrial Lon Protease and the Importance of Its N-Domain

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dc.contributor.author Adam, C en
dc.contributor.author Picard, M en
dc.contributor.author Déquard-Chablat, M en
dc.contributor.author Sellem, CH en
dc.contributor.author Denmat, SH-L en
dc.contributor.author Contamine, V en
dc.contributor.editor Lee, Y-W en
dc.date.accessioned 2019-11-04T02:42:38Z en
dc.date.issued 2012-05-31 en
dc.identifier.citation PLoS ONE 7(5):10 pages Article number e38138 31 May 2012 en
dc.identifier.issn 1932-6203 en
dc.identifier.uri http://hdl.handle.net/2292/48813 en
dc.description.abstract Mitochondria have their own ATP-dependent proteases that maintain the functional state of the organelle. All multicellular eukaryotes, including filamentous fungi, possess the same set of mitochondrial proteases, unlike in unicellular yeasts, where ClpXP, one of the two matricial proteases, is absent. Despite the presence of ClpXP in the filamentous fungus Podospora anserina, deletion of the gene encoding the other matricial protease, PaLon1, leads to lethality at high and low temperatures, indicating that PaLON1 plays a main role in protein quality control. Under normal physiological conditions, the PaLon1 deletion is viable but decreases life span. PaLon1 deletion also leads to defects in two steps during development, ascospore germination and sexual reproduction, which suggests that PaLON1 ensures important regulatory functions during fungal development. Mitochondrial Lon proteases are composed of a central ATPase domain flanked by a large non-catalytic N-domain and a C-terminal protease domain. We found that three mutations in the N-domain of PaLON1 affected fungal life cycle, PaLON1 protein expression and mitochondrial proteolytic activity, which reveals the functional importance of the N-domain of the mitochondrial Lon protease. All PaLon1 mutations affected the C-terminal part of the N-domain. Considering that the C-terminal part is predicted to have an α helical arrangement in which the number, length and position of the helices are conserved with the solved structure of its bacterial homologs, we propose that this all-helical structure participates in Lon substrate interaction. en
dc.publisher Public Library of Science (PLoS) en
dc.relation.ispartofseries PLoS ONE en
dc.rights Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. en
dc.rights.uri https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm en
dc.rights.uri https://creativecommons.org/licenses/by/4.0/ en
dc.title Biological Roles of the Podospora anserina Mitochondrial Lon Protease and the Importance of Its N-Domain en
dc.type Journal Article en
dc.identifier.doi 10.1371/journal.pone.0038138 en
pubs.issue 5 en
pubs.volume 7 en
dc.rights.holder Copyright: The authors en
pubs.publication-status Published en
dc.rights.accessrights http://purl.org/eprint/accessRights/OpenAccess en
pubs.subtype Article en
pubs.elements-id 756554 en
dc.identifier.eissn 1932-6203 en
pubs.number e38138 en
pubs.record-created-at-source-date 2018-11-24 en
pubs.online-publication-date 2012-05-31 en


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