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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2002-5-28
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pubmed:abstractText |
Histone H2A has been found to be efficient in DNA delivery into a number of cell lines. We have reasoned that this DNA-delivery activity is mediated by two mechanisms: (i) electrostatically driven DNA binding and condensation by histone and (ii) nuclear import of these histone H2A.DNA polyplexes via nuclear localization signals in the protein. We have identified a 37-aa N-terminal peptide of histone H2A that is active in in vitro gene transfer. This peptide can function as a nuclear localization signal and can bind DNA. Amino acid substitutions that replace positively charged residues and/or DNA-binding residues of this peptide obliterate transfection activity. The introduction of a proline in the first turn of an alpha-helix of this 37-mer obliterates transfection activity, suggesting that the integrity of the alpha-helical structure of the N-terminal region of histone H2A is related to its transfection activity.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12032306-10195264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12032306-10751040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12032306-11016973,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12032306-11807406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12032306-3123916,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12032306-7754385,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12032306-8760902,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12032306-8844198,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12032306-8865814,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12032306-9095402,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12032306-9163942,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12032306-9202069,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12032306-9231075,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12032306-9305837,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12032306-9371635,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12032306-9407553,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12032306-9434155
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
99
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7467-71
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12032306-Amino Acid Sequence,
pubmed-meshheading:12032306-Animals,
pubmed-meshheading:12032306-COS Cells,
pubmed-meshheading:12032306-Cell Line,
pubmed-meshheading:12032306-Cell Nucleus,
pubmed-meshheading:12032306-Cercopithecus aethiops,
pubmed-meshheading:12032306-Gene Transfer Techniques,
pubmed-meshheading:12032306-Histones,
pubmed-meshheading:12032306-Molecular Sequence Data,
pubmed-meshheading:12032306-Peptide Fragments,
pubmed-meshheading:12032306-Protein Transport,
pubmed-meshheading:12032306-Recombinant Proteins,
pubmed-meshheading:12032306-Static Electricity,
pubmed-meshheading:12032306-Transfection
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pubmed:year |
2002
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pubmed:articleTitle |
Structure and function correlation in histone H2A peptide-mediated gene transfer.
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pubmed:affiliation |
Department of Molecular and Experimental Medicine, The Scripps Research Institute, 10550 North Torrey Pines Road, MEM 215, La Jolla, CA 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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