# name
Biophysical characterization of the association of histones with
                single-stranded DNA

# metadata.dc.description.abstract[].value
BACKGROUND: Despite the profound current knowledge of the
                architecture and dynamics of nucleosomes, little is known about
                the structures generated by the interaction of histones with
                single-stranded DNA (ssDNA), which is widely present during
                replication and transcription. METHODS: Non-denaturing gel
                electrophoresis, transmission electron microscopy, atomic force
                microscopy, magnetic tweezers. RESULTS: Histones have a high
                affinity for ssDNA at physiological salt concentrations, with an
                apparent binding constant similar to that calculated for their
                association with double-stranded DNA (dsDNA). The length of DNA
                (number of nucleotides in ssDNA or base pairs in dsDNA)
                associated with a fixed core histone mass is the same for both
                ssDNA and dsDNA. Whereas histone-ssDNA complexes show a high
                tendency to aggregate in 0.2 M NaCl, at lower ionic strength
                nucleosome-like structures are formed. Core histones are able to
                protect ssDNA from digestion by micrococcal nuclease, and a
                shortening of ssDNA occurs upon its interaction with histones.
                The purified (+) strand of a cloned DNA fragment of nucleosomal
                origin has a higher affinity for histones than the purified
                complementary (-) strand. CONCLUSIONS: At physiological ionic
                strength histones have high affinity for ssDNA, possibly
                associating with it into nucleosome-like structures. General
                Significance In the cell nucleus histones may spontaneously
                interact with ssDNA to facilitate their participation in the
                replication and transcription of chromatin.

# metadata.dc.relation.isformatof[].value
Versió postprint del document publicat a:
                http://dx.doi.org/10.1016/j.bbagen.2017.07.018

# metadata.dc.relation.ispartof[].value
Biochimica et Biophysica Acta. General Subjects, 2017

# metadata.dc.source[].value
Articles publicats en revistes (ISGlobal)

# metadata.dc.title[].value
Biophysical characterization of the association of histones with
                single-stranded DNA