BibTex format
@article{Garnett:2015:10.1002/pro.2640,
author = {Garnett, JA and Muhl, D and Douse, CH and Hui, K and Busch, A and Omisore, A and Yang, Y and Simpson, P and Marchant, J and Waksman, G and Matthews, S and Filloux, A},
doi = {10.1002/pro.2640},
journal = {Protein Science},
pages = {670--687},
title = {Structure-function analysis reveals that the Pseudomonas aeruginosa Tps4 two-partner secretion system is involved in CupB5 translocation},
url = {http://dx.doi.org/10.1002/pro.2640},
volume = {24},
year = {2015}
}
RIS format (EndNote, RefMan)
TY - JOUR
AB - Pseudomonas aeruginosa is a Gram-negative opportunistic bacterium, synonymous withcystic fibrosis patients, which can cause chronic infection of the lungs. This pathogen is a modelorganism to study biofilms: a bacterial population embedded in an extracellular matrix that provideprotection from environmental pressures and lead to persistence. A number of Chaperone-UsherPathways, namely CupA-CupE, play key roles in these processes by assembling adhesive pili onthe bacterial surface. One of these, encoded by the cupB operon, is unique as it contains anonchaperone-usher gene product, CupB5. Two-partner secretion (TPS) systems are comprised ofa C-terminal integral membrane b-barrel pore with tandem N-terminal POTRA (POlypeptide TRansportAssociated) domains located in the periplasm (TpsB) and a secreted substrate (TpsA). UsingNMR we show that TpsB4 (LepB) interacts with CupB5 and its predicted cognate partner TpsA4(LepA), an extracellular protease. Moreover, using cellular studies we confirm that TpsB4 cantranslocate CupB5 across the P. aeruginosa outer membrane, which contrasts a previous observationthat suggested the CupB3 P-usher secretes CupB5. In support of our findings we also demonstratethat tps4/cupB operons are coregulated by the RocS1 sensor suggesting P. aeruginosa hasdeveloped synergy between these systems. Furthermore, we have determined the solutionstructureof the TpsB4-POTRA1 domain and together with restraints from NMR chemical shift mappingand in vivo mutational analysis we have calculated models for the entire TpsB4 periplasmic region in complex with both TpsA4 and CupB5 secretion motifs. The data highlight specific residuesfor TpsA4/CupB5 recognition by TpsB4 in the periplasm and suggest distinct roles for eachPOTRA domain.
AU - Garnett,JA
AU - Muhl,D
AU - Douse,CH
AU - Hui,K
AU - Busch,A
AU - Omisore,A
AU - Yang,Y
AU - Simpson,P
AU - Marchant,J
AU - Waksman,G
AU - Matthews,S
AU - Filloux,A
DO - 10.1002/pro.2640
EP - 687
PY - 2015///
SN - 1469-896X
SP - 670
TI - Structure-function analysis reveals that the Pseudomonas aeruginosa Tps4 two-partner secretion system is involved in CupB5 translocation
T2 - Protein Science
UR - http://dx.doi.org/10.1002/pro.2640
VL - 24
ER -
