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- W2742844218 endingPage "74" @default.
- W2742844218 startingPage "61" @default.
- W2742844218 abstract "Pathogenicity of the gram-negative bacterium Xanthomonas campestris pv. vesicatoria depends on a type III secretion (T3S) system, which translocates effector proteins into plant cells. Effector proteins contain N-terminal T3S and translocation signals and interact with the T3S chaperone HpaB, which presumably escorts effectors to the secretion apparatus. The molecular mechanisms underlying the recognition of effectors by the T3S system are not yet understood. In the present study, we analyzed T3S and translocation signals in the type III effectors XopE2 and XopJ from X. campestris pv. vesicatoria. Both effectors contain minimal translocation signals, which are only recognized in the absence of HpaB. Additional N-terminal signals promote translocation of XopE2 and XopJ in the wild-type strain. The results of translocation and interaction studies revealed that the interaction of XopE2 and XopJ with HpaB and a predicted cytoplasmic substrate docking site of the T3S system is not sufficient for translocation. In agreement with this finding, we show that the presence of an artificial HpaB-binding site does not promote translocation of the noneffector XopA in the wild-type strain. Our data, therefore, suggest that the T3S chaperone HpaB not only acts as an escort protein but also controls the recognition of translocation signals." @default.
- W2742844218 created "2017-08-17" @default.
- W2742844218 creator A5015850951 @default.
- W2742844218 creator A5018051004 @default.
- W2742844218 creator A5044838107 @default.
- W2742844218 creator A5050164204 @default.
- W2742844218 creator A5055624829 @default.
- W2742844218 creator A5084172665 @default.
- W2742844218 date "2018-01-01" @default.
- W2742844218 modified "2023-09-26" @default.
- W2742844218 title "The Type III Secretion Chaperone HpaB Controls the Translocation of Effector and Noneffector Proteins From <i>Xanthomonas campestris</i> pv. <i>vesicatoria</i>" @default.
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