DNA binding properties of the purified Antennapedia homeodomain.

作者：Markus Affolter, Anthony Percival‐Smith, Martin Müller, Werner Leupin, W J Gehring · 发表于：Proceedings of the National Academy of Sciences · 年份：1990 · DOI：10.1073/pnas.87.11.4093 · 被引用次数：193 · 研究领域：Genomics and Chromatin Dynamics、Epigenetics and DNA Methylation、Bacterial Genetics and Biotechnology

The in vitro DNA binding properties of a purified 68-amino acid Antennapedia homeodomain (Antp HD) peptide have been analyzed. Equilibrium and kinetic binding studies showed that stable DNA-protein complexes are formed with a Kd of 1.6 x 10(-9) M and 1.8 x 10(-10) M, respectively. Heterodimer analysis led to the conclusion that Antp HD interacts in vitro as a monomer with the DNA target sites used in our study. The results of methylation and ethylation interference studies indicated that the Antp HD closely approaches the target DNA primarily from one side in a region extending across three phosphate backbones. The DNA binding properties of the Antp HD and prokaryotic DNA binding domains that share a helix-turn-helix motif are compared.