A tandem repeat of the SPKK peptide motif induces psi-type DNA structures at alternating AT sequences.
The interaction between a tandem repeat of the SPKK peptide motif and calf thymus DNA or several polynucleotides has been investigated by circular dichroism. The octapeptide SPKKSPKK does not induce any important changes in the CD spectra of the polynucleotides poly(dG).poly(dC), poly(dG-dC).poly(dG-dC) and poly(dA).poly(dT) while the spectrum of calf thymus DNA is slightly modified. Binding of this basic peptide to the alternating copolymer poly(dA-dT).poly(dA-dT) results in a marked psi-type condensation in a manner similar to that induced by the entire C-terminal domain of histone H1.
INSERM Unité 124, Institut de Recherches sur le Cancer, Lille, France.
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Bailly
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Colson
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Houssier
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Hénichart
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D004247:DNA / Q000187:drug effects* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000494:pharmacology*; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation / Q000187:drug effects; D009842:Oligopeptides / Q000494:pharmacology*; D011067:Poly dA-dT / Q000737:chemistry* / Q000378:metabolism; D011089:Polydeoxyribonucleotides / Q000737:chemistry / Q000378:metabolism; D012091:Repetitive Sequences, Nucleic Acid
D004268:DNA-Binding Proteins; D009842:Oligopeptides; D011089:Polydeoxyribonucleotides; C059837:seryl-prolyl-lysyl-lysine; D011067:Poly dA-dT; D004247:DNA