dc.contributor.author |
Wang, Ying |
dc.contributor.author |
Merwyk, Luis Van |
dc.contributor.author |
Tönsing, Katja |
dc.contributor.author |
Walhorn, Volker |
dc.contributor.author |
Anselmetti, Dario |
dc.contributor.author |
Fernàndez Busquets, Xavier |
dc.date |
2017-09-26T10:54:45Z |
dc.date |
2018-07-27T22:01:20Z |
dc.date |
2017-07-27 |
dc.date |
2017-08-30T18:00:31Z |
dc.identifier.citation |
0006-3002 |
dc.identifier.uri |
http://hdl.handle.net/2445/115793 |
dc.format |
29 p. |
dc.format |
application/pdf |
dc.language.iso |
eng |
dc.publisher |
Elsevier |
dc.relation |
Versió postprint del document publicat a:
http://dx.doi.org/10.1016/j.bbagen.2017.07.018 |
dc.relation |
Biochimica et Biophysica Acta. General Subjects, 2017 |
dc.relation |
http://dx.doi.org/10.1016/j.bbagen.2017.07.018 |
dc.rights |
cc-by-nc-nd (c) Elsevier, 2017 |
dc.rights |
info:eu-repo/semantics/openAccess |
dc.rights |
http://creativecommons.org/licenses/by-nc-nd/3.0/es |
dc.subject |
Histones |
dc.subject |
Cromatina |
dc.subject |
Histones |
dc.subject |
Chromatine |
dc.title |
Biophysical characterization of the association of histones with
single-stranded DNA |
dc.type |
info:eu-repo/semantics/article |
dc.type |
info:eu-repo/semantics/acceptedVersion |
dc.description.abstract |
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. |