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Structure and function correlation in histone H2A peptide-mediated gene transfer.

Danuta Balicki·Christopher D Putnam·Puthupparampil V Scaria·Ernest Beutler
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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 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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Amino Acid SequenceAnimalsCOS CellsCell LineCell NucleusChlorocebus aethiopsGene Transfer TechniquesHistonesMolecular Sequence DataPeptide FragmentsProtein TransportRecombinant ProteinsStatic ElectricityTransfectionJournal ArticleResearch Support, Non-U.S. Gov't

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Danuta Balicki, Christopher D Putnam, Puthupparampil V Scaria, Ernest Beutler. 2002-05-28. Structure and function correlation in histone H2A peptide-mediated gene transfer.. https://doi.org/10.1073/pnas.102168299

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