Negatively charged lipid membranes promote a disorder-order transition in the Yersinia YscU protein.

ABSTRACT: The inner membrane of Gram-negative bacteria is negatively charged, rendering positively charged cytoplasmic proteins in close proximity likely candidates for protein-membrane interactions. YscU is a Yersinia pseudotuberculosis type III secretion system protein crucial for bacterial pathogenesis. The protein contains a highly conserved positively charged linker sequence that separates membrane-spanning and cytoplasmic (YscUC) domains. Although disordered in solution, inspection of the primary sequence of the linker reveals that positively charged residues are separated with a typical helical periodicity. Here, we demonstrate that the linker sequence of YscU undergoes a largely electrostatically driven coil-to-helix transition upon binding to negatively charged membrane interfaces. Using me

SUBMITTER: Weise CF 

PROVIDER: S-EPMC4213669 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature