Customized secretion chaperones in pathogenic bacteria

摘要: Pathogenic yersiniae secrete about a dozen anti-host proteins, the Yops, by pathway which does not involve cleavage of classical signal peptide. The Yop secretory apparatus, called Ysc, for secretion, is archetype type III secretion systems (which serve virulence proteins several animal and plant pathogens) related to flagellar assembly apparatus. N-terminal but has been defined date. Apart from Ysc machinery, at least four Yops requires cytoplasmic Syc (for specific chaperone). Each protein binds its cognate Yop. Unlike most chaperones, these do have an ATP-binding domain, are presumably devoid ATPase activity. They share few common properties: acidic pl, size in range 15-20 kDa, putative amphipathic alpha-helix C-terminal portion. were recently shown counterparts other pathogenic bacteria, where they appear similar function.