The intrinsically disordered nature of the peroxisomal protein translocation machinery. (1st December 2018)

• Record Type: Journal Article
• Authors: Barros‐Barbosa, Aurora; Rodrigues, Tony A.; Ferreira, Maria J.; Pedrosa, Ana G.; Teixeira, Nélson R.; Francisco, Tânia; Azevedo, Jorge E.
• Is Part Of: FEBS journal. Volume 286:Number 1(2019)
• Page Start: 24
• Page End: 38
• Publication Date: 2018-12-01
• Subjects: docking/translocation module -- intrinsic disorder -- matrix protein import -- peroxins -- peroxisomes; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pathology, Molecular -- Periodicals; 572
• DOI: 10.1111/febs.14704
• Languages: English
• ISSNs: 1742-464X

Abstract

Abstract : 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. Abstract : In order to translocate a wide range of already folded proteins, the peroxisomal matrix protein import machinery must be flexible. Unsurprisingly, several of its key components have large intrinsically disordered domains. In this review, we provide an overview on these domains and their interactions, trying to infer their functional roles in this protein sorting pathway.