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Folding Control in the Path of Type 5 Secretion

Authors :
Nathalie Dautin
Laboratoire de biologie physico-chimique des protéines membranaires (LBPC-PM (UMR_7099))
Institut de biologie physico-chimique (IBPC (FR_550))
Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP)
Source :
Toxins, Toxins, Vol 13, Iss 341, p 341 (2021), Toxins, MDPI, 2021, 13 (5), pp.341. ⟨10.3390/toxins13050341⟩
Publication Year :
2021
Publisher :
MDPI, 2021.

Abstract

International audience; The type 5 secretion system (T5SS) is one of the more widespread secretion systems in Gram-negative bacteria. Proteins secreted by the T5SS are functionally diverse (toxins, adhesins, enzymes) and include numerous virulence factors. Mechanistically, the T5SS has long been considered the simplest of secretion systems, due to the paucity of proteins required for its functioning. Still, despite more than two decades of study, the exact process by which T5SS substrates attain their final destination and correct conformation is not totally deciphered. Moreover, the recent addition of new sub-families to the T5SS raises additional questions about this secretion mechanism. Central to the understanding of type 5 secretion is the question of protein folding, which needs to be carefully controlled in each of the bacterial cell compartments these proteins cross. Here, the biogenesis of proteins secreted by the Type 5 secretion system is discussed, with a focus on the various factors preventing or promoting protein folding during biogenesis.

Details

Language :
English
ISSN :
20726651
Volume :
13
Issue :
5
Database :
OpenAIRE
Journal :
Toxins
Accession number :
edsair.doi.dedup.....f09f35ca31db88949e978439d81748cc
Full Text :
https://doi.org/10.3390/toxins13050341⟩