Interactions among the sevenHelicobacter pyloriproteins encoded by the urease gene cluster

Autor: David L. Weeks, Petra Voland, Elizabeth A. Marcus, George Sachs, Christian Prinz, David R. Scott
Rok vydání: 2003
Předmět:
Zdroj: American Journal of Physiology-Gastrointestinal and Liver Physiology. 284:G96-G106
ISSN: 1522-1547
0193-1857
DOI: 10.1152/ajpgi.00160.2002
Popis: Survival of Helicobacter pylori in acid depends on intrabacterial urease. This urease is a Ni2+-containing oligomeric heterodimer. Regulation of its activity and assembly is important for gastric habitation by this neutralophile. The gene complex encodes catalytic subunits ( ureA/B), an acid-gated urea channel ( ureI), and accessory assembly proteins ( ureE–H). With the use of yeast two-hybrid analysis for determining protein-protein interactions, UreF as bait identified four interacting sequences encoding UreH, whereas UreG as bait detected five UreE sequences. These results were confirmed by coimmunoprecipitation and β-galactosidase assays. Native PAGE immunoblotting of H. pylori inner membranes showed interaction of UreA/B with UreI, whereas UreI deletion mutants lacked this protein interaction. Deletion of ureE–H did not affect this interaction with UreI. Hence, the accessory proteins UreE/G and UreF/H form dimeric complexes and UreA/B form a membrane complex with UreI, perhaps enabling assembly of the urease apoenzyme at the membrane surface and immediate urea access to intrabacterial urease to allow rapid periplasmic neutralization.
Databáze: OpenAIRE