May 29, 2002

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

Proceedings of the National Academy of Sciences of the United States of America
Danuta BalickiErnest Beutler

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.

Mentioned in this Paper

Nuclear Import
Histone antigen
Transfection
Molecular Helix
Gene Transfer Techniques
Static Electricity
Proteins, Recombinant DNA
COS-7 Cells
Helix (Snails)
Proline

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