Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1977-7-18
|
| pubmed:abstractText |
The interactions of DNA with the five histone components (H1, H2B, H2A, H3 and H4) and with a number of histone fragments (N-H1 (1--72), C-H1 (73--216), N-H2B (l--59), C-H2B, (63--125), N-H2A (1-39), C-H2A (58--129), N-H4 (1--84) and C-H4 (85--102) have been studied by using the techniques of thermal denaturation and solubility behaviour. Complexes in 10(-3) M phosphate buffer, 2 - 10(-5) M Na(2)-EDTA, pH 7.0 were prepared by the direct mixing method. For lysine-rich histones (H1 and H2B) it has been found that the main characteristics which governs the interaction with DNA are located in the very lysine-rich part of the molecules, i.e. in the C-H1 and N-H2B segments. These regions are also responsible for a cooperative distribution of the histone along the DNA molecules in the artificial complexes. It appears from our studies that the tertiary structure of the moderately, arginine-rich histone (H2A) is an essential feature for its interaction with DNA. The two arginine-rich histones (H3 and H4) complexed with DNA behave in a similar way, both in thermal denaturation and in DNA precipitation. In the case of C-H4, a marked shift of the melting profile has been observed which is correlated with the presence in the peptide of the hydrophilic cluster Lys-Arg-Gln-Gly-Arg-Thr. Our results suggest that large segments rich in lysine and basic clustering within histones give rise to different modes of electrostatic interaction with DNA.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0006-3002
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
17
|
| pubmed:volume |
476
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
108-21
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:861226-Animals,
pubmed-meshheading:861226-Cattle,
pubmed-meshheading:861226-Chemical Phenomena,
pubmed-meshheading:861226-Chemistry,
pubmed-meshheading:861226-DNA,
pubmed-meshheading:861226-Histones,
pubmed-meshheading:861226-Hot Temperature,
pubmed-meshheading:861226-Nucleic Acid Denaturation,
pubmed-meshheading:861226-Osmolar Concentration,
pubmed-meshheading:861226-Peptide Fragments,
pubmed-meshheading:861226-Protein Conformation,
pubmed-meshheading:861226-Sodium Chloride,
pubmed-meshheading:861226-Solubility,
pubmed-meshheading:861226-Thymus Gland
|
| pubmed:year |
1977
|
| pubmed:articleTitle |
Interactions of histones and histone peptides with DNA Thermal denaturation and solubility studies.
|
| pubmed:publicationType |
Journal Article
|