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The intrinsically disordered nature of the peroxisomal protein translocation machinery
Author(s) -
BarrosBarbosa Aurora,
Rodrigues Tony A.,
Ferreira Maria J.,
Pedrosa Ana G.,
Teixeira Nélson R.,
Francisco Tânia,
Azevedo Jorge E.
Publication year - 2019
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14704
Subject(s) - peroxisome , protein targeting , cytosol , organelle , microbiology and biotechnology , sorting , membrane protein , chemistry , cytoplasm , membrane , chromosomal translocation , biology , computational biology , biochemistry , gene , computer science , enzyme , programming language
Despite having a membrane that is impermeable to all but the smallest of metabolites, peroxisomes acquire their newly synthesized (cytosolic) matrix proteins in an already folded conformation. In some cases, even oligomeric proteins have been reported to translocate the organelle membrane. The protein sorting machinery that accomplishes this feat must be rather flexible and, unsurprisingly, several of its key components have large intrinsically disordered domains. Here, we provide an overview on these domains and their interactions trying to infer their functional roles in this protein sorting pathway.