Heterochiral Jun and Fos bZIP peptides form a coiled ‐coil heterodimer that is competent for DNA binding

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.

Coiled‐coil interaction plays important roles in regulation of transcription, cell differentiation, and cell growth. The d‐l heterochiral Jun–Fos heterodimer formation induced DNA binding and showed conformational change by DNA binding.

Source: Journal of Peptide Science - February 9, 2017 Category: Biochemistry Authors: Rui Kamada, Natsumi Nakagawa, Taiji Oyama, Kazuyasu Sakaguchi Tags: Special Issue Article Source Type: research