title: Heterochiral Jun and Fos bZIP peptides form a coiled-coil heterodimer that is competent for DNA binding.
abstract: Coiled coils, consisting of at least two α-helices, have important roles in the regulation of transcription, cell differentiation, and cell growth. Peptides composed of d-amino acids (d-peptides) have received great attention for their potential in biomedical applications, because they give large diversity for the design of peptidyl drug and are more resistant to proteolytic digestion than l-peptides. However, the interactions between l-peptides/l-protein and d-peptides in the formation of complex are poorly understood. In this study, stereoisomer-specific peptides were constructed corresponding to regions of the basic-leucine-zipper domains of Jun and Fos proteins. basic-leucine-zipper domains consist of an N-terminal basic domain, which is responsible for DNA binding, and a C-terminal domain that enables homodimerization or heterodimerization via formation of a coiled-coil. By combining peptides with different stereochemistries, the d-l heterochiral Jun-Fos heterodimer formation induced DNA binding by the basic domains of Jun-Fos. Our study provides new insight into the interaction between l-peptide and d-peptide enantiomers for developing d-peptide materials and drugs. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.
authors.affiliation: Laboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo, 060-0810, Japan.
authors.forename: Rui
authors.initials: R
authors.lastname: Kamada
authors.affiliation: Laboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo, 060-0810, Japan.
authors.forename: Natsumi
authors.initials: N
authors.lastname: Nakagawa
authors.affiliation: Laboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo, 060-0810, Japan.
authors.forename: Taiji
authors.initials: T
authors.lastname: Oyama
authors.affiliation: Laboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo, 060-0810, Japan.
authors.forename: Kazuyasu
authors.initials: K
authors.lastname: Sakaguchi
mesh_terms: D000595:Amino Acid Sequence; D050976:Basic-Leucine Zipper Transcription Factors / Q000737:chemistry*; D002942:Circular Dichroism; D019281:Dimerization; D024202:Electrophoretic Mobility Shift Assay; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D016760:Proto-Oncogene Proteins c-fos / Q000737:chemistry*; D016755:Proto-Oncogene Proteins c-jun / Q000737:chemistry*
chemical_list: D050976:Basic-Leucine Zipper Transcription Factors; D010455:Peptides; D016760:Proto-Oncogene Proteins c-fos; D016755:Proto-Oncogene Proteins c-jun
keywords: DNA binding; coiled-coil; d-peptide; heterodimer; leucine zipper