Tetratricopeptide repeats are essential for PcrH chaperone function in Pseudomonas aeruginosa type III secretion.

Abstract:

:The type III secretion system (T3SS) is a specialized apparatus evolved by Gram-negative bacteria to deliver effector proteins into host cells, thus facilitating the establishment of an infection. Effector translocation across the target cell plasma membrane is believed to occur via pores formed by at least two secreted translocator proteins, the functions of which are dependent upon customized class II T3SS chaperones. Recently, three internal tetratricopeptide repeats (TPRs) were identified in this class of chaperones. Here, defined mutagenesis of the class II chaperone PcrH of Pseudomonas aeruginosa revealed these TPRs to be essential for chaperone activity towards the translocator proteins PopB and PopD and subsequently for the translocation of exoenzymes into host cells.

journal_name

FEMS Microbiol Lett

authors

Bröms JE,Edqvist PJ,Forsberg A,Francis MS

doi

10.1111/j.1574-6968.2005.00099.x

keywords:

subject

Has Abstract

pub_date

2006-03-01 00:00:00

pages

57-66

issue

1

eissn

0378-1097

issn

1574-6968

pii

FML099

journal_volume

256

pub_type

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