Source:http://linkedlifedata.com/resource/pubmed/id/11551189
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
37
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pubmed:dateCreated |
2001-9-11
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pubmed:abstractText |
Poly(ADP-ribosyl)ation of nuclear proteins is responsible for major changes in the high-order chromatin structure. The effects of this post-translation modification on nuclear architecture were examined at different Mg2+ concentrations using scanning force microscopy. A quantitative analysis of the internucleosomal distance, the width, and the volume of chromatin fibers imaged in tapping mode reveals that poly(ADP-ribosyl)ation induces a complete relaxation and decondensation of the chromatin structure. Our data, on the center-to-center distance between adjacent nucleosomes and on the fiber width, indicate that the poly(ADP-ribosyl)ated fibers remain significantly decondensed even in the presence of Mg2+. Our results also show that the Mg2+ assumes an important role in the folding of chromatin structure, but Mg2+ is not able to restore the native feature of chromatin, when the fibers are depleted of H1/H5 histones. The combined effect of post-translation modification and cation ions on the chromatin structure shows that poly(ADP-ribosyl)ation could promote accessibility to DNA even in those nuclear processes that require Mg2+.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleosomes,
http://linkedlifedata.com/resource/pubmed/chemical/Poly Adenosine Diphosphate Ribose
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
40
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10947-55
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11551189-Chromatin,
pubmed-meshheading:11551189-Histones,
pubmed-meshheading:11551189-Magnesium,
pubmed-meshheading:11551189-Microscopy, Atomic Force,
pubmed-meshheading:11551189-Molecular Conformation,
pubmed-meshheading:11551189-Nucleosomes,
pubmed-meshheading:11551189-Poly Adenosine Diphosphate Ribose,
pubmed-meshheading:11551189-Protein Processing, Post-Translational
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pubmed:year |
2001
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pubmed:articleTitle |
Effect of poly(ADP-ribosyl)ation and Mg2+ ions on chromatin structure revealed by scanning force microscopy.
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pubmed:affiliation |
Department of Biochemical Sciences, University of La Sapienza, P.le A. Moro 5, I-00185 Roma, Italy. maria.derme@uniroma1.it
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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