title: General interaction mode of CIDE:CIDE complex revealed by a mutation study of the Drep2 CIDE domain.
abstract: The CIDE domain is a well known protein-protein interaction module that is initially detected at the apoptotic DNA fragmentation factor (DFF40/45). The interaction mechanism via the CIDE domain is not well understood. To elucidate CIDE domain mediated interactions in the apoptotic DNA fragmentation system, we conducted biochemical and mutational studies and found that the surface of CIDE domains can be divided into an acidic side and a basic side. In addition, a mutagenesis study revealed that the basic surface side of Drep2 CIDE is involved in the interaction with the acidic surface side of Drep1 CIDE and Drep3 CIDE. Our research supports the idea that a charge-charge interaction might be the general interaction mode of the CIDE:CIDE interaction.
authors.affiliation: School of Biotechnology and Graduate School of Biochemistry, Yeungnam University, Gyeongsan, Republic of Korea.
authors.forename: Seung Mi
authors.initials: SM
authors.lastname: Lee
authors.forename: Hyun Ho
authors.initials: HH
authors.lastname: Park
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D051017:Apoptosis Regulatory Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D029721:Drosophila Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D004331:Drosophila melanogaster / Q000235:genetics / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D011485:Protein Binding / Q000235:genetics; D054730:Protein Interaction Domains and Motifs / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D013499:Surface Properties
chemical_list: D051017:Apoptosis Regulatory Proteins; C402282:Drep2 protein, Drosophila; C402283:Drep3 protein, Drosophila; D029721:Drosophila Proteins; C109664:caspase-activated DNase inhibitor