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 Lettjournal_title
FEMS microbiology lettersauthors
Bröms JE,Edqvist PJ,Forsberg A,Francis MSdoi
10.1111/j.1574-6968.2005.00099.xkeywords:
subject
Has Abstractpub_date
2006-03-01 00:00:00pages
57-66issue
1eissn
0378-1097issn
1574-6968pii
FML099journal_volume
256pub_type
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