Continuous and pulsed hydrogen-deuterium exchange and mass spectrometry characterize CsgE oligomerization.

ABSTRACT: We report the use of hydrogen-deuterium amide exchange coupled to mass spectrometry (HDX-MS) to study the interfaces of and conformational changes accompanying CsgE oligomerization. This protein plays an important role in enteric bacteria biofilm formation. Biofilms provide protection for enteric bacteria from environmental extremes and raise concerns about controlling bacteria and infectious disease. Their proteinaceous components, called curli, are extracellular functional amyloids that initiate surface contact and biofilm formation. The highly regulated curli biogenesis involves a major subunit, CsgA, a minor subunit CsgB, and a series of other accessory proteins. CsgE, possibly functioning as oligomer, is a chaperonin-like protein that delivers CsgA to an outer-membrane bound oligomeri

SUBMITTER: Wang H 

PROVIDER: S-EPMC4761447 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature