Biophysical characterization of the association of histones with single-stranded DNA
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. Non-denaturing gel electrophoresis, tr...
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| Published in | Biochimica et biophysica acta. General subjects Vol. 1861; no. 11; pp. 2739 - 2749 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
01.11.2017
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| Subjects | |
| Online Access | Get full text |
| ISSN | 0304-4165 1872-8006 |
| DOI | 10.1016/j.bbagen.2017.07.018 |
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| Abstract | 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.
Non-denaturing gel electrophoresis, transmission electron microscopy, atomic force microscopy, magnetic tweezers.
Histones have a high affinity for ssDNA in 0.15M NaCl ionic strength, 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. Although histone-ssDNA complexes show a high tendency to aggregate, nucleosome-like structures are formed at physiological salt concentrations. 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.
At physiological ionic strength histones have high affinity for ssDNA, possibly associating with it into nucleosome-like structures.
In the cell nucleus histones may spontaneously interact with ssDNA to facilitate their participation in the replication and transcription of chromatin.
•Histones have high affinity for single-stranded DNA at physiological ionic strength.•A fixed core histone mass complexes equal lengths of single- and double-stranded DNAs.•Histones shorten the length of single-stranded DNA in magnetic tweezers assays.•Nucleosome-like structures might be formed by histones and single-stranded DNA. |
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| AbstractList | 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.Non-denaturing gel electrophoresis, transmission electron microscopy, atomic force microscopy, magnetic tweezers.Histones have a high affinity for ssDNA in 0.15M NaCl ionic strength, 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. Although histone-ssDNA complexes show a high tendency to aggregate, nucleosome-like structures are formed at physiological salt concentrations. 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.At physiological ionic strength histones have high affinity for ssDNA, possibly associating with it into nucleosome-like structures.In the cell nucleus histones may spontaneously interact with ssDNA to facilitate their participation in the replication and transcription of chromatin. 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. Non-denaturing gel electrophoresis, transmission electron microscopy, atomic force microscopy, magnetic tweezers. Histones have a high affinity for ssDNA in 0.15M NaCl ionic strength, 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. Although histone-ssDNA complexes show a high tendency to aggregate, nucleosome-like structures are formed at physiological salt concentrations. 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. At physiological ionic strength histones have high affinity for ssDNA, possibly associating with it into nucleosome-like structures. In the cell nucleus histones may spontaneously interact with ssDNA to facilitate their participation in the replication and transcription of chromatin. 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.BACKGROUNDDespite 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.Non-denaturing gel electrophoresis, transmission electron microscopy, atomic force microscopy, magnetic tweezers.METHODSNon-denaturing gel electrophoresis, transmission electron microscopy, atomic force microscopy, magnetic tweezers.Histones have a high affinity for ssDNA in 0.15M NaCl ionic strength, 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. Although histone-ssDNA complexes show a high tendency to aggregate, nucleosome-like structures are formed at physiological salt concentrations. 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.RESULTSHistones have a high affinity for ssDNA in 0.15M NaCl ionic strength, 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. Although histone-ssDNA complexes show a high tendency to aggregate, nucleosome-like structures are formed at physiological salt concentrations. 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.At physiological ionic strength histones have high affinity for ssDNA, possibly associating with it into nucleosome-like structures.CONCLUSIONSAt physiological ionic strength histones have high affinity for ssDNA, possibly associating with it into nucleosome-like structures.In the cell nucleus histones may spontaneously interact with ssDNA to facilitate their participation in the replication and transcription of chromatin.GENERAL SIGNIFICANCEIn the cell nucleus histones may spontaneously interact with ssDNA to facilitate their participation in the replication and transcription of chromatin. 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. Non-denaturing gel electrophoresis, transmission electron microscopy, atomic force microscopy, magnetic tweezers. Histones have a high affinity for ssDNA in 0.15M NaCl ionic strength, 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. Although histone-ssDNA complexes show a high tendency to aggregate, nucleosome-like structures are formed at physiological salt concentrations. 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. At physiological ionic strength histones have high affinity for ssDNA, possibly associating with it into nucleosome-like structures. In the cell nucleus histones may spontaneously interact with ssDNA to facilitate their participation in the replication and transcription of chromatin. •Histones have high affinity for single-stranded DNA at physiological ionic strength.•A fixed core histone mass complexes equal lengths of single- and double-stranded DNAs.•Histones shorten the length of single-stranded DNA in magnetic tweezers assays.•Nucleosome-like structures might be formed by histones and single-stranded DNA. |
| Author | Wang, Ying Anselmetti, Dario Walhorn, Volker Fernàndez-Busquets, Xavier van Merwyk, Luis Tönsing, Katja |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/28756274$$D View this record in MEDLINE/PubMed |
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| Keywords | Histones Magnetic tweezers Electrophoresis Single-stranded DNA Force spectroscopy Nucleosome |
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| SubjectTerms | atomic force microscopy Biophysical Phenomena Cell Nucleus - chemistry Cell Nucleus - genetics Chromatin - chemistry Chromatin - genetics digestion DNA fragmentation DNA Replication - genetics DNA, Single-Stranded - chemistry DNA, Single-Stranded - genetics Electrophoresis Force spectroscopy gel electrophoresis Histones Histones - chemistry Histones - genetics ionic strength Magnetic tweezers magnetism micrococcal nuclease Nucleosome nucleosomes Nucleosomes - chemistry Nucleosomes - genetics nucleotides Osmolar Concentration Single-stranded DNA sodium chloride transmission electron microscopy |
| Title | Biophysical characterization of the association of histones with single-stranded DNA |
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