Folding Control in the Path of Type 5 Secretion

被引:9
作者
Dautin, Nathalie [1 ,2 ]
机构
[1] Univ Paris, Lab Biol Physicochim Prot Membranaires, LBPC PM, CNRS,UMR7099, F-75005 Paris, France
[2] Fdn Edmond Rothschild Dev Rech Sci, Inst Biol Physicochim, F-75005 Paris, France
关键词
secretion; folding; autotransporter; type 5 secretion system; intimin; invasin; two-partner secretion; trimeric autotransporter; EXTENDED SIGNAL PEPTIDE; OUTER-MEMBRANE PROTEIN; TRIMERIC AUTOTRANSPORTER ADHESIN; ESCHERICHIA-COLI; 2-PARTNER SECRETION; STRUCTURAL BASIS; PERIPLASMIC CHAPERONES; RECOGNITION PARTICLE; BACTERIAL PROTEIN; PASSENGER DOMAIN;
D O I
10.3390/toxins13050341
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
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.
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页数:21
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