Abstract
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 α-helix of this 37-mer obliterates transfection activity, suggesting that the integrity of the α-helical structure of the N-terminal region of histone H2A is related to its transfection activity.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 26, 2002, 10:46 a.m.) |
Deposited | 3 years, 4 months ago (April 12, 2022, 7:38 p.m.) |
Indexed | 11 months, 2 weeks ago (Sept. 12, 2024, 1:09 a.m.) |
Issued | 23 years, 3 months ago (May 28, 2002) |
Published | 23 years, 3 months ago (May 28, 2002) |
Published Online | 23 years, 3 months ago (May 28, 2002) |
Published Print | 23 years, 3 months ago (May 28, 2002) |
@article{Balicki_2002, title={Structure and function correlation in histone H2A peptide-mediated gene transfer}, volume={99}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.102168299}, DOI={10.1073/pnas.102168299}, number={11}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Balicki, Danuta and Putnam, Christopher D. and Scaria, Puthupparampil V. and Beutler, Ernest}, year={2002}, month=may, pages={7467–7471} }