The essentials of protein import in the degenerate mitochondrion of Entamoeba histolytica.

Several essential biochemical processes are situated in mitochondria. The metabolic transformation of mitochondria in distinct lineages of eukaryotes created proteomes ranging from thousands of proteins to what appear to be a much simpler scenario. In the case of Entamoeba histolytica, tiny mitochon...

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Autores principales:	Pavel Dolezal, Michael J Dagley, Maya Kono, Peter Wolynec, Vladimir A Likić, Jung Hock Foo, Miroslava Sedinová, Jan Tachezy, Anna Bachmann, Iris Bruchhaus, Trevor Lithgow
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/953953f7b9624adf836cb8eaec47afad
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spelling	oai:doaj.org-article:953953f7b9624adf836cb8eaec47afad2021-11-25T05:48:14ZThe essentials of protein import in the degenerate mitochondrion of Entamoeba histolytica.1553-73661553-737410.1371/journal.ppat.1000812https://doaj.org/article/953953f7b9624adf836cb8eaec47afad2010-03-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20333239/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Several essential biochemical processes are situated in mitochondria. The metabolic transformation of mitochondria in distinct lineages of eukaryotes created proteomes ranging from thousands of proteins to what appear to be a much simpler scenario. In the case of Entamoeba histolytica, tiny mitochondria known as mitosomes have undergone extreme reduction. Only recently a single complete metabolic pathway of sulfate activation has been identified in these organelles. The E. histolytica mitosomes do not produce ATP needed for the sulfate activation pathway and for three molecular chaperones, Cpn60, Cpn10 and mtHsp70. The already characterized ADP/ATP carrier would thus be essential to provide cytosolic ATP for these processes, but how the equilibrium of inorganic phosphate could be maintained was unknown. Finally, how the mitosomal proteins are translocated to the mitosomes had remained unclear. We used a hidden Markov model (HMM) based search of the E. histolytica genome sequence to discover candidate (i) mitosomal phosphate carrier complementing the activity of the ADP/ATP carrier and (ii) membrane-located components of the protein import machinery that includes the outer membrane translocation channel Tom40 and membrane assembly protein Sam50. Using in vitro and in vivo systems we show that E. histolytica contains a minimalist set up of the core import components in order to accommodate a handful of mitosomal proteins. The anaerobic and parasitic lifestyle of E. histolytica has produced one of the simplest known mitochondrial compartments of all eukaryotes. Comparisons with mitochondria of another amoeba, Dictystelium discoideum, emphasize just how dramatic the reduction of the protein import apparatus was after the loss of archetypal mitochondrial functions in the mitosomes of E. histolytica.Pavel DolezalMichael J DagleyMaya KonoPeter WolynecVladimir A LikićJung Hock FooMiroslava SedinováJan TachezyAnna BachmannIris BruchhausTrevor LithgowPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 6, Iss 3, p e1000812 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Pavel Dolezal Michael J Dagley Maya Kono Peter Wolynec Vladimir A Likić Jung Hock Foo Miroslava Sedinová Jan Tachezy Anna Bachmann Iris Bruchhaus Trevor Lithgow The essentials of protein import in the degenerate mitochondrion of Entamoeba histolytica.
description	Several essential biochemical processes are situated in mitochondria. The metabolic transformation of mitochondria in distinct lineages of eukaryotes created proteomes ranging from thousands of proteins to what appear to be a much simpler scenario. In the case of Entamoeba histolytica, tiny mitochondria known as mitosomes have undergone extreme reduction. Only recently a single complete metabolic pathway of sulfate activation has been identified in these organelles. The E. histolytica mitosomes do not produce ATP needed for the sulfate activation pathway and for three molecular chaperones, Cpn60, Cpn10 and mtHsp70. The already characterized ADP/ATP carrier would thus be essential to provide cytosolic ATP for these processes, but how the equilibrium of inorganic phosphate could be maintained was unknown. Finally, how the mitosomal proteins are translocated to the mitosomes had remained unclear. We used a hidden Markov model (HMM) based search of the E. histolytica genome sequence to discover candidate (i) mitosomal phosphate carrier complementing the activity of the ADP/ATP carrier and (ii) membrane-located components of the protein import machinery that includes the outer membrane translocation channel Tom40 and membrane assembly protein Sam50. Using in vitro and in vivo systems we show that E. histolytica contains a minimalist set up of the core import components in order to accommodate a handful of mitosomal proteins. The anaerobic and parasitic lifestyle of E. histolytica has produced one of the simplest known mitochondrial compartments of all eukaryotes. Comparisons with mitochondria of another amoeba, Dictystelium discoideum, emphasize just how dramatic the reduction of the protein import apparatus was after the loss of archetypal mitochondrial functions in the mitosomes of E. histolytica.
format	article
author	Pavel Dolezal Michael J Dagley Maya Kono Peter Wolynec Vladimir A Likić Jung Hock Foo Miroslava Sedinová Jan Tachezy Anna Bachmann Iris Bruchhaus Trevor Lithgow
author_facet	Pavel Dolezal Michael J Dagley Maya Kono Peter Wolynec Vladimir A Likić Jung Hock Foo Miroslava Sedinová Jan Tachezy Anna Bachmann Iris Bruchhaus Trevor Lithgow
author_sort	Pavel Dolezal
title	The essentials of protein import in the degenerate mitochondrion of Entamoeba histolytica.
title_short	The essentials of protein import in the degenerate mitochondrion of Entamoeba histolytica.
title_full	The essentials of protein import in the degenerate mitochondrion of Entamoeba histolytica.
title_fullStr	The essentials of protein import in the degenerate mitochondrion of Entamoeba histolytica.
title_full_unstemmed	The essentials of protein import in the degenerate mitochondrion of Entamoeba histolytica.
title_sort	essentials of protein import in the degenerate mitochondrion of entamoeba histolytica.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/953953f7b9624adf836cb8eaec47afad
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The essentials of protein import in the degenerate mitochondrion of Entamoeba histolytica.

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