Analysis of interaction of mitochondrial outer membrane translocator TOM40 complex using <em>in vivo</em> site-specific photocrosslinking — ASN Events
  1. Schedule
  2. Session 12: Poster Session D - Including Happy Hour & Trade Display
  3. Analysis of interaction of mitochondrial outer membrane translocator TOM40 complex using in vivo site-specific photocrosslinking

Analysis of interaction of mitochondrial outer membrane translocator TOM40 complex using in vivo site-specific photocrosslinking (#435)

Takuya Shiota 1 , Kenichirou Imai 2 , Noriyuki Sakiyama 2 , Megumi Kamiya 3 , Yoshironi Fukasawa 2 , Kentaro Tomii 2 , Chai Kua 1 , Toshiya Endo 3 , Paul Horton 2 , Trevor Lithgow 1
  1. Monash University, Clayton, VIC, Australia
  2. AIST, CBRC, Tokyo, Japan
  3. Nagoya University, Nagoya, Aichi, Japana

Newly synthesized precursor proteins are imported via the TOM40 complex. The TOM40 complex consists of the channel forming protein Tom40, the three receptor proteins (Tom20, Tom22 and Tom70), and small Tom proteins (Tom5, Tom6 and Tom7). TOM40 complex forms 440 kDa complex. Structure of TOM40 complex were analysed by cryo-EM, but the specific binding region of subunits of TOM40 complex are still unclear. In order to understand the specific binding region of  subunits each other and stoichiometry of TOM40 complex, we employed in vivo site-specific photocrosslinking to Tom22, Tom20, Tom7, and Tom40. Moreover the results of crosslink experiments of Tom40 were adopted to modeling structure of Tom40 which is made from crystal structure of VDAC-1 (1). 

The cytosolic domain of Tom20 interacts with Tom22 and Tom40. The transmembrane segments of Tom22 and Tom7 interact with Tom40. Tom40 interacts with Tom22, Tom20 and Tim10.

  1. [1] Ujwal R, et al (2008) The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating. Proc Natl Acad Sci U S A. 105, 17742-7.