Structure and function correlation in histone H2A peptide-mediated gene transfer
AUTOR(ES)
Balicki, Danuta
FONTE
The National Academy of Sciences
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=124254Documentos Relacionados
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