Functional relationship of FliS and HP1076 in flagellar export
Refereed conference paper presented and published in conference proceedings

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AbstractHelicobacter pylori is the main cause of peptic ulcer and a primary risk factor for gastric adenocarcinoma. To colonize the gastric environment, H. pylori must be motile. Motility is conferred by complex nanomachines which consists of membrane-associated and cytoplasmic proteins that construct an apparatus with an export pore, through which the flagella type III secretion system governs the precise delivery of flagellar proteins. In model microorganisms E. coli and Salmonella, export chaperones FlgN, FliS and FliT act as ‘bodyguards’ to protect their specific protein substrate(s) from premature polymerization in the cytosol and pilot them to the export apparatus in a timely manner. However, accumulated genetics and structural studies have demonstrated the divergence of the flagellar system in diverse bacteria. To date, the molecular basis of flagellar export in H. pylori is not well understood. Although FliS interacts with flagellins in model bacteria, we recently, determined that H. pylori FliS has several additional interaction partners. This outcome suggests that FliS may have a broad substrate spectrum and perform multiple functions. Here, we report our findings of FliS and its interacting partners by a combination of molecular genetics and structural biology approaches.
All Author(s) ListLAM Wendy Wai Ling, ZHANG Huawei, SUN Kailei, AU Shannon Wing Ngor
Name of ConferenceEMBO EMBL Symposium 2017: New Approaches and Concepts in Microbiology
Start Date of Conference27/06/2017
End Date of Conference30/06/2017
Place of ConferenceHeidelberg
Country/Region of ConferenceGermany
LanguagesEnglish-United States

Last updated on 2018-11-05 at 16:37