'SPKK' motifs prefer to bind to DNA at A/T-rich sites.
The termini of histone H1 and sea urchin spermatogenous H1 and H2B, which are essential for correct chromatin condensation, often contain repeats of the sequence SPK(R)K(R). A special type of beta-turn structural motif has been proposed for this sequence, and it has been shown that a segment of the sea urchin sperm H1 N terminus, which has six repeats of the motif (S6 peptide), binds to DNA and competes with the DNA binding drug Hoechst 33258. Here, we demonstrate by quantitative analysis of hydroxyl radical footprints that the synthetic oligopeptide, SPRKSPRK (S2), and the S6 peptide prefer to bind to the minor groove of DNA at the same A/T-rich sites. The locations of these binding sites are similar to Hoechst, but the sequence specificity of the oligopeptides is lower than that of Hoechst, and the detailed protection patterns differ slightly. We suggest that these small peptides and Hoechst recognize similar sequence-dependent features of the local architecture of DNA.
Churchill
M E
ME
MRC Laboratory of Molecular Biology, Cambridge, UK.
Suzuki
M
M
D000225:Adenine; D000595:Amino Acid Sequence; D000818:Animals; D001482:Base Composition; D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000378:metabolism*; D005609:Free Radicals; D006657:Histones / Q000378:metabolism*; D006878:Hydroxides; D017665:Hydroxyl Radical; D008297:Male; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D012617:Sea Urchins; D013094:Spermatozoa / Q000378:metabolism; D013941:Thymine
D005609:Free Radicals; D006657:Histones; D006878:Hydroxides; D017665:Hydroxyl Radical; D004247:DNA; D000225:Adenine; D013941:Thymine