Structural and functional characterization of the TIM23 complex
The main focus of our research is structural and functional characterization of the TIM23 complex, the major protein translocase of the mitochondrial inner membrane.
The vast majority of mitochondrial proteins are encoded in the nuclear genome, synthesized in the cytosol in form of precursor proteins and subsequently transported into one of the four mitochondrial subcompartments, the outer membrane, the inner membrane, the intermembrane space and the matrix.
The TIM23 complex is the major protein translocase of the mitochondrial inner membrane. It uses the energy of membrane potential across the mitochondrial inner membrane and ATP in the matrix to transport proteins across and insert them into the inner membrane. The TIM23 complex consists of at least ten subunits, eight of which are essential for viability of yeast cells and are highly conserved throughout the eukaryotic kingdom. Recently, mutations in the subunits of the TIM23 complex were also implicated in various human disorders.