Histone proteins provide a structural framework so that genomic DNA can be reversibly compacted within the limited volume of the cell. The interactions of dsDNA with histone monomers to form the extended, cross-linked histone:DNA structures known as chromatin have been well-studied. Interactions between ssDNA and histones, vital during DNA replication and RNA transcription, are less well-studied. We used a combination of dye-labelled, sub-100 nucleotide-long ssDNA oligomer rulers, F�rster-resonance energy transfer (FRET) and quasi-elastic light scattering (QELS) to probe the structural evolution of ssDNA:histone assemblies. FRET measurements revealed an exponential oligomer length-dependent signal while QELS measurements showed the evolution, with changes of oligomer length, of structures with characteristic sizes. Both results were consistent with ssDNA-stabilization of histone monomers into octamers and eventual cross-linking into chromatin-like structures.

Exploring the dramatic dependence of ssDNA:histone assembly on oligomer length

244th National Meeting (2012)

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