Hetero-oligomer of dynamin-related proteins participates in the fission of highly divergent mitochondria from Entamoeba histolytica

Abstract Entamoeba histolytica is an anaerobic parasitic protist and possesses mitosomes, one of the most highly divergent mitochondrion-related organelles (MROs). Although unique metabolism and protein/metabolite transport machinery have been demonstrated in Entamoeba mitosomes, the mechanism of mi...

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Autores principales:	Takashi Makiuchi, Herbert J. Santos, Hiroshi Tachibana, Tomoyoshi Nozaki
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/61d77d68a9534dc5ab7aa2c083bb3748
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spelling	oai:doaj.org-article:61d77d68a9534dc5ab7aa2c083bb37482021-12-02T15:06:05ZHetero-oligomer of dynamin-related proteins participates in the fission of highly divergent mitochondria from Entamoeba histolytica10.1038/s41598-017-13721-52045-2322https://doaj.org/article/61d77d68a9534dc5ab7aa2c083bb37482017-10-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-13721-5https://doaj.org/toc/2045-2322Abstract Entamoeba histolytica is an anaerobic parasitic protist and possesses mitosomes, one of the most highly divergent mitochondrion-related organelles (MROs). Although unique metabolism and protein/metabolite transport machinery have been demonstrated in Entamoeba mitosomes, the mechanism of mitosomal fusion and fission remains to be elucidated. In this study, we demonstrate that two dynamin-related proteins (DRPs) are cooperatively involved in the fission of Entamoeba mitosomes. Expression of a dominant negative form of EhDrpA and EhDrpB, and alternatively, repression of gene expression of EhDrpA and EhDrpB genes, caused elongation of mitosomes, reflecting inhibition of mitosomal fission. Moreover, EhDrpA and EhDrpB formed an unprecedented hetero-oligomeric complex with an approximate 1:2 to 1:3 ratio, suggesting that the observed elongation of mitosomes is likely caused by the disruption and instability of the complex caused by an imbalance in the two DRPs. Altogether, this is the first report of a hetero-oligomeric DRP complex which participates in the fission of mitochondria and MROs.Takashi MakiuchiHerbert J. SantosHiroshi TachibanaTomoyoshi NozakiNature 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 Takashi Makiuchi Herbert J. Santos Hiroshi Tachibana Tomoyoshi Nozaki Hetero-oligomer of dynamin-related proteins participates in the fission of highly divergent mitochondria from Entamoeba histolytica
description	Abstract Entamoeba histolytica is an anaerobic parasitic protist and possesses mitosomes, one of the most highly divergent mitochondrion-related organelles (MROs). Although unique metabolism and protein/metabolite transport machinery have been demonstrated in Entamoeba mitosomes, the mechanism of mitosomal fusion and fission remains to be elucidated. In this study, we demonstrate that two dynamin-related proteins (DRPs) are cooperatively involved in the fission of Entamoeba mitosomes. Expression of a dominant negative form of EhDrpA and EhDrpB, and alternatively, repression of gene expression of EhDrpA and EhDrpB genes, caused elongation of mitosomes, reflecting inhibition of mitosomal fission. Moreover, EhDrpA and EhDrpB formed an unprecedented hetero-oligomeric complex with an approximate 1:2 to 1:3 ratio, suggesting that the observed elongation of mitosomes is likely caused by the disruption and instability of the complex caused by an imbalance in the two DRPs. Altogether, this is the first report of a hetero-oligomeric DRP complex which participates in the fission of mitochondria and MROs.
format	article
author	Takashi Makiuchi Herbert J. Santos Hiroshi Tachibana Tomoyoshi Nozaki
author_facet	Takashi Makiuchi Herbert J. Santos Hiroshi Tachibana Tomoyoshi Nozaki
author_sort	Takashi Makiuchi
title	Hetero-oligomer of dynamin-related proteins participates in the fission of highly divergent mitochondria from Entamoeba histolytica
title_short	Hetero-oligomer of dynamin-related proteins participates in the fission of highly divergent mitochondria from Entamoeba histolytica
title_full	Hetero-oligomer of dynamin-related proteins participates in the fission of highly divergent mitochondria from Entamoeba histolytica
title_fullStr	Hetero-oligomer of dynamin-related proteins participates in the fission of highly divergent mitochondria from Entamoeba histolytica
title_full_unstemmed	Hetero-oligomer of dynamin-related proteins participates in the fission of highly divergent mitochondria from Entamoeba histolytica
title_sort	hetero-oligomer of dynamin-related proteins participates in the fission of highly divergent mitochondria from entamoeba histolytica
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/61d77d68a9534dc5ab7aa2c083bb3748
work_keys_str_mv	AT takashimakiuchi heterooligomerofdynaminrelatedproteinsparticipatesinthefissionofhighlydivergentmitochondriafromentamoebahistolytica AT herbertjsantos heterooligomerofdynaminrelatedproteinsparticipatesinthefissionofhighlydivergentmitochondriafromentamoebahistolytica AT hiroshitachibana heterooligomerofdynaminrelatedproteinsparticipatesinthefissionofhighlydivergentmitochondriafromentamoebahistolytica AT tomoyoshinozaki heterooligomerofdynaminrelatedproteinsparticipatesinthefissionofhighlydivergentmitochondriafromentamoebahistolytica
_version_	1718388585691873280

Hetero-oligomer of dynamin-related proteins participates in the fission of highly divergent mitochondria from Entamoeba histolytica

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