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 $\alpha$-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.
%0 Journal Article
%1 pusnikEssentialNovelComponent2012a
%A Pusnik, Mascha
%A Mani, Jan
%A Schmidt, Oliver
%A Niemann, Moritz
%A Oeljeklaus, Silke
%A Schnarwiler, Felix
%A Warscheid, Bettina
%A Lithgow, Trevor
%A Meisinger, Chris
%A Schneider, André
%C United States
%D 2012
%J Molecular biology of the cell
%K Cell Interference,RNA Interfering,to_read,Trypanosoma Line,Mitochondria/metabolism,Mitochondrial Membrane Membranes/*metabolism,Mitochondrial Proteins/chemistry/*metabolism,Mitochondrial Proteins/chemistry/genetics/*metabolism,RNA Proteins/chemistry/genetics/metabolism,Protein Small Transport Transport,Protozoan brucei brucei/genetics/*metabolism/ultrastructure
%N 17
%P 3420--3428
%R 10.1091/mbc.E12-02-0107
%T An Essential Novel Component of the Noncanonical Mitochondrial Outer Membrane Protein Import System of Trypanosomatids.
%V 23
%X 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 $\alpha$-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.
@article{pusnikEssentialNovelComponent2012a,
abstract = {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 {$\alpha$}-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.},
added-at = {2024-05-17T13:01:35.000+0200},
address = {United States},
author = {Pusnik, Mascha and Mani, Jan and Schmidt, Oliver and Niemann, Moritz and Oeljeklaus, Silke and Schnarwiler, Felix and Warscheid, Bettina and Lithgow, Trevor and Meisinger, Chris and Schneider, Andr{\'e}},
biburl = {https://www.bibsonomy.org/bibtex/2c4f2a5788c2f1cd0fbc1edae9fa2df23/warscheidlab},
doi = {10.1091/mbc.E12-02-0107},
interhash = {f45b74476893a0609ef5ea1b488674a2},
intrahash = {c4f2a5788c2f1cd0fbc1edae9fa2df23},
issn = {1939-4586 1059-1524},
journal = {Molecular biology of the cell},
keywords = {Cell Interference,RNA Interfering,to_read,Trypanosoma Line,Mitochondria/metabolism,Mitochondrial Membrane Membranes/*metabolism,Mitochondrial Proteins/chemistry/*metabolism,Mitochondrial Proteins/chemistry/genetics/*metabolism,RNA Proteins/chemistry/genetics/metabolism,Protein Small Transport Transport,Protozoan brucei brucei/genetics/*metabolism/ultrastructure},
langid = {english},
month = sep,
number = 17,
pages = {3420--3428},
pmcid = {PMC3431924},
pmid = {22787278},
timestamp = {2024-05-17T13:01:35.000+0200},
title = {An Essential Novel Component of the Noncanonical Mitochondrial Outer Membrane Protein Import System of Trypanosomatids.},
volume = 23,
year = 2012
}