Interaction mode of CIDE family proteins in fly: DREP1 and DREP3 acidic surfaces interact with DREP2 and DREP4 basic surfaces

• DOI: 10.1371/journal.pone.0189819
• Publication Date: 2017-12-14T13:44:19Z
• Authors: Chang Min Kim; Sun Hee Jeon; Jun-Hyuk Choi; Jun Hyuck Lee; Hyun Ho Park
• Keywords: Fragmentation

Cell death-inducing DNA fragmentation factor 45 (DFF45)-like effector (CIDE) domains were initially identified as protein interaction modules in apoptotic nucleases and are now known to form a highly conserved family with diverse functions that range from cell death lipid homeostasis. In the fly, four CIDE domain-containing proteins (DFF-related [DREP]-1–4) their functions, including relationships, have been identified. this study, we introduced investigated acidic side-disrupted mutants of DREP1, DREP2, DREP3. We discovered surface patches DREP1 DREP3 critical for homo-dimerization. addition, found sides interact basic DREP2 DREP4. Our current study provides clear evidence demonstrating mechanism interactions between DREP fly.