Research: Project 1

Chaperone-assisted membrane protein folding

YidC/Oxa1/Alb3 is a membrane protein family that plays a critical role in folding and assembly of membrane proteins in the inner membranes of bacteria, mitochondria, and chloroplasts. In E. coli, YidC forms a membrane insertion pore independent of SecYEG complex, major protein translocation machinery. YidC also has a chaperone activity: it facilitates the folding of a variety of SecYEG-dependent proteins. To understand how YidC acts as chaperone, we will tackle three specific problems.

  • What are the driving forces in YidC-substrate interaction?
  • How does YidC facilitate folding of membrane proteins?
  • How are the structure and dynamics of YidC related to the function?