A conserved glycine residue of trimeric autotransporter domains plays a key role in Yersinia adhesin A autotransport. Export

@article{citeulike:2713048, abstract = {The Yersinia adhesin A (YadA) is a trimeric autotransporter adhesin of enteric yersiniae. It consists of three major domains: a head mediating adherence to host cells, a stalk involved in serum resistance, and an anchor that forms a membrane pore and is responsible for the autotransport function. The anchor contains a glycine residue, nearly invariant throughout trimeric autotransporter adhesins, that faces the pore lumen. To address the role of this glycine, we replaced it with polar amino acids of increasing side chain size and expressed wild-type and mutant YadA in Escherichia coli. The mutations did not impair the YadA-mediated adhesion to collagen and to host cells or the host cell cytokine production, but they decreased the expression levels and stability of YadA trimers with increasing side chain size. Likewise, autoagglutination and resistance to serum were decreased in these mutants. We found that the periplasmic protease DegP is involved in the degradation of YadA and that in an E. coli degP deletion strain, mutant versions of YadA were expressed almost to wild-type levels. We conclude that the conserved glycine residue affects both the export and the stability of YadA and consequently some of its putative functions in pathogenesis.}, address = {Institut f\"{u}r Medizinische Mikrobiologie und Hygiene, Universit\"{a}tsklinikum T\"{u}bingen, T\"{u}bingen, Germany.}, author = {Grosskinsky, Ulrike and Sch\"{u}tz, Monika and Fritz, Michaela and Schmid, Yvonne and Lamparter, Marina C. and Szczesny, Pawel and Lupas, Andrei N. and Autenrieth, Ingo B. and Linke, Dirk}, citeulike-article-id = {2713048}, citeulike-linkout-0 = {http://dx.doi.org/10.1128/JB.00985-07}, citeulike-linkout-1 = {http://jb.asm.org/content/189/24/9011.abstract}, citeulike-linkout-2 = {http://jb.asm.org/content/189/24/9011.full.pdf}, citeulike-linkout-3 = {http://view.ncbi.nlm.nih.gov/pubmed/17921300}, citeulike-linkout-4 = {http://www.hubmed.org/display.cgi?uids=17921300}, day = {15}, doi = {10.1128/JB.00985-07}, issn = {1098-5530}, journal = {Journal of bacteriology}, keywords = {gly, glycine}, month = {December}, number = {24}, pages = {9011--9019}, posted-at = {2009-10-28 04:22:01}, priority = {2}, title = {A conserved glycine residue of trimeric autotransporter domains plays a key role in Yersinia adhesin A autotransport.}, url = {http://dx.doi.org/10.1128/JB.00985-07}, volume = {189}, year = {2007} }

TY - JOUR ID - citeulike:2713048 L3 - citeulike-article-id:2713048 N2 - The Yersinia adhesin A (YadA) is a trimeric autotransporter adhesin of enteric yersiniae. It consists of three major domains: a head mediating adherence to host cells, a stalk involved in serum resistance, and an anchor that forms a membrane pore and is responsible for the autotransport function. The anchor contains a glycine residue, nearly invariant throughout trimeric autotransporter adhesins, that faces the pore lumen. To address the role of this glycine, we replaced it with polar amino acids of increasing side chain size and expressed wild-type and mutant YadA in Escherichia coli. The mutations did not impair the YadA-mediated adhesion to collagen and to host cells or the host cell cytokine production, but they decreased the expression levels and stability of YadA trimers with increasing side chain size. Likewise, autoagglutination and resistance to serum were decreased in these mutants. We found that the periplasmic protease DegP is involved in the degradation of YadA and that in an E. coli degP deletion strain, mutant versions of YadA were expressed almost to wild-type levels. We conclude that the conserved glycine residue affects both the export and the stability of YadA and consequently some of its putative functions in pathogenesis. IS - 24 JF - Journal of bacteriology SN - 1098-5530 AD - Institut für Medizinische Mikrobiologie und Hygiene, Universitätsklinikum Tübingen, Tübingen, Germany. EP - 9019 TI - A conserved glycine residue of trimeric autotransporter domains plays a key role in Yersinia adhesin A autotransport. VL - 189 SP - 9011 KW - gly KW - glycine AU - Grosskinsky, Ulrike AU - Schütz, Monika AU - Fritz, Michaela AU - Schmid, Yvonne AU - Lamparter, Marina AU - Szczesny, Pawel AU - Lupas, Andrei AU - Autenrieth, Ingo AU - Linke, Dirk PY - 2007/12/15/ UR - http://dx.doi.org/10.1128/JB.00985-07 ER -