Tetratricopeptide repeats are essential for PcrH chaperone function in Pseudomonas aeruginosa type III secretion.
2006 (English)In: FEMS Microbiol Lett, ISSN 0378-1097, Vol. 256, no 1, 57-66 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2006. Vol. 256, no 1, 57-66 p.
ADP Ribose Transferases/secretion, Antibodies; Monoclonal/metabolism, Bacterial Proteins/metabolism/*physiology/*secretion, Bacterial Toxins, Gene Expression Regulation; Bacterial/genetics/*physiology, Hela Cells, Humans, Immunoblotting/methods, Molecular Chaperones/chemistry/genetics/*physiology, Molecular Sequence Data, Mutagenesis; Site-Directed/methods, Phenotype, Pore Forming Cytotoxic Proteins/metabolism/secretion, Pseudomonas aeruginosa/genetics/*physiology, Sequence Alignment, Sequence Analysis; Protein, Time Factors, Two-Hybrid System Techniques
IdentifiersURN: urn:nbn:se:umu:diva-16669PubMedID: 16487320OAI: oai:DiVA.org:umu-16669DiVA: diva2:156342