Dresden 2017 – scientific programme

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BP: Fachverband Biologische Physik

BP 10: Posters - Single Molecule Biophysics

BP 10.8: Poster

Monday, March 20, 2017, 17:30–19:30, P3

Biophysical investigation of the association of histones with double- and single-stranded DNA — Ying Wang¹, •Dennis Kreft¹, Luis van Merwyk¹, Katja Tönsing¹, Volker Walhorn¹, Xavier Fernàndez-Busquets², and Dario Anselmetti¹ — ¹Experimental Biophysics and Applied Nanoscience, Faculty of Physics, Bielefeld University, Bielefeld, Germany — ²Institute for Bioengineering of Catalonia and Barcelona Institute for Global Health, Barcelona, Spain

Nucleosome formation is the process of how nucleic dsDNA is packed in eukaryotes. Nucleosome core particles consist of 147 bp of dsDNA, which wrapped in 1.67 left-handed superhelical turns around a histone octamer, consisting of 2 copies each of the core histones (H2A, H2B, H3, H4) and stabilized by the linker histone H1, forming the well-known ``beads on a string" chromatin structure. Despite many studies of histones associating with dsDNA, little is known about the structures generated by the interaction of histones with ssDNA. In this work, we employed magnetic tweezers (MT) and atomic force microscopy (AFM) to investigate the association of histones with dsDNA and ssDNA. For ssDNA in the presence of histones, the results of MT assays indicate a shortening of ssDNA upon its interaction with histones as well as AFM imaging exhibits a compacted ssDNA structure. Compared with the characteristics of histones-dsDNA binding, these data suggest that histones and ssDNA associate into some type of nucleosome-like assembly that may facilitate the participation of histones in the replication and transcription of chromatin.