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An essential novel component of the noncanonical mitochondrial outer membrane protein import system of trypanosomatids

The mitochondrial outer membrane protein Tom40 is the general entry gate for imported proteins in essentially all eukaryotes. Trypanosomatids lack Tom40, however, and use instead a protein termed the archaic translocase of the outer mitochondrial membrane (ATOM). Here we report the discovery of pATO...

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Autores principales: Pusnik, Mascha, Mani, Jan, Schmidt, Oliver, Niemann, Moritz, Oeljeklaus, Silke, Schnarwiler, Felix, Warscheid, Bettina, Lithgow, Trevor, Meisinger, Chris, Schneider, André
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3431924/
https://www.ncbi.nlm.nih.gov/pubmed/22787278
http://dx.doi.org/10.1091/mbc.E12-02-0107
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author Pusnik, Mascha
Mani, Jan
Schmidt, Oliver
Niemann, Moritz
Oeljeklaus, Silke
Schnarwiler, Felix
Warscheid, Bettina
Lithgow, Trevor
Meisinger, Chris
Schneider, André
author_facet Pusnik, Mascha
Mani, Jan
Schmidt, Oliver
Niemann, Moritz
Oeljeklaus, Silke
Schnarwiler, Felix
Warscheid, Bettina
Lithgow, Trevor
Meisinger, Chris
Schneider, André
author_sort Pusnik, Mascha
collection PubMed
description The mitochondrial outer membrane protein Tom40 is the general entry gate for imported proteins in essentially all eukaryotes. Trypanosomatids lack Tom40, however, and use instead a protein termed the archaic translocase of the outer mitochondrial membrane (ATOM). Here we report the discovery of pATOM36, a novel essential component of the trypanosomal outer membrane protein import system that interacts with ATOM. pATOM36 is not related to known Tom proteins from other organisms and mediates the import of matrix proteins. However, there is a group of precursor proteins whose import is independent of pATOM36. Domain-swapping experiments indicate that the N-terminal presequence-containing domain of the substrate proteins at least in part determines the dependence on pATOM36. Secondary structure profiling suggests that pATOM36 is composed largely of α-helices and its assembly into the outer membrane is independent of the sorting and assembly machinery complex. Taken together, these results show that pATOM36 is a novel component associated with the ATOM complex that promotes the import of a subpopulation of proteins into the mitochondrial matrix.
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spelling pubmed-34319242012-11-16 An essential novel component of the noncanonical mitochondrial outer membrane protein import system of trypanosomatids Pusnik, Mascha Mani, Jan Schmidt, Oliver Niemann, Moritz Oeljeklaus, Silke Schnarwiler, Felix Warscheid, Bettina Lithgow, Trevor Meisinger, Chris Schneider, André Mol Biol Cell Articles The mitochondrial outer membrane protein Tom40 is the general entry gate for imported proteins in essentially all eukaryotes. Trypanosomatids lack Tom40, however, and use instead a protein termed the archaic translocase of the outer mitochondrial membrane (ATOM). Here we report the discovery of pATOM36, a novel essential component of the trypanosomal outer membrane protein import system that interacts with ATOM. pATOM36 is not related to known Tom proteins from other organisms and mediates the import of matrix proteins. However, there is a group of precursor proteins whose import is independent of pATOM36. Domain-swapping experiments indicate that the N-terminal presequence-containing domain of the substrate proteins at least in part determines the dependence on pATOM36. Secondary structure profiling suggests that pATOM36 is composed largely of α-helices and its assembly into the outer membrane is independent of the sorting and assembly machinery complex. Taken together, these results show that pATOM36 is a novel component associated with the ATOM complex that promotes the import of a subpopulation of proteins into the mitochondrial matrix. The American Society for Cell Biology 2012-09-01 /pmc/articles/PMC3431924/ /pubmed/22787278 http://dx.doi.org/10.1091/mbc.E12-02-0107 Text en © 2012 Pusnik et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell BD; are registered trademarks of The American Society of Cell Biology.
spellingShingle Articles
Pusnik, Mascha
Mani, Jan
Schmidt, Oliver
Niemann, Moritz
Oeljeklaus, Silke
Schnarwiler, Felix
Warscheid, Bettina
Lithgow, Trevor
Meisinger, Chris
Schneider, André
An essential novel component of the noncanonical mitochondrial outer membrane protein import system of trypanosomatids
title An essential novel component of the noncanonical mitochondrial outer membrane protein import system of trypanosomatids
title_full An essential novel component of the noncanonical mitochondrial outer membrane protein import system of trypanosomatids
title_fullStr An essential novel component of the noncanonical mitochondrial outer membrane protein import system of trypanosomatids
title_full_unstemmed An essential novel component of the noncanonical mitochondrial outer membrane protein import system of trypanosomatids
title_short An essential novel component of the noncanonical mitochondrial outer membrane protein import system of trypanosomatids
title_sort essential novel component of the noncanonical mitochondrial outer membrane protein import system of trypanosomatids
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3431924/
https://www.ncbi.nlm.nih.gov/pubmed/22787278
http://dx.doi.org/10.1091/mbc.E12-02-0107
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