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- W86385217 abstract "Research Article1 March 1989free access SPKK, a new nucleic acid-binding unit of protein found in histone. M. Suzuki M. Suzuki Laboratory of Neurochemistry, National Institute for Physiological Sciences, Okazaki, Japan. Search for more papers by this author M. Suzuki M. Suzuki Laboratory of Neurochemistry, National Institute for Physiological Sciences, Okazaki, Japan. Search for more papers by this author Author Information M. Suzuki1 1Laboratory of Neurochemistry, National Institute for Physiological Sciences, Okazaki, Japan. The EMBO Journal (1989)8:797-804https://doi.org/10.1002/j.1460-2075.1989.tb03440.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info A new DNA-binding unit of a protein different from the alpha-helix, the beta-sheet and the Zn-finger is proposed based on the analysis of the structure of the N-terminus of sea urchin spermatogenous histone H1. DNA-binding arms of the sea urchin spermatogenous histones, H1 and H2B, are composed of repeats of Ser-Pro-Lys(Arg)-Lys(Arg) (SPKK) residues. A six-times repeat of SPKK (S6 peptide) was isolated from H1 and the competition of S6 for DNA binding with a DNA-binding dye, Hoechst 33258, was analysed. The S6 peptide is shown to be a competitive inhibitor of Hoechst 33258, and it is concluded that the SPKK repeat binds to DNA in its minor groove with a binding constant, KS6 = 1.67 X 10(10) M-1. The circular dichroism (CD) spectrum of a synthetic peptide, SPRKSPRK (S2 peptide), is quite different from those of both the alpha-helix and the beta-sheet and resembles that of a random coil. From statistical consideration of protein structures it is proposed that SPKK forms a compact beta-turn stabilized by an additional hydrogen bond. Since a repeated chain of such turn of SPKK offers a repeat of amides of Ser residues at a distance similar to that of DNA-binding amides of the drugs, Hoechst 33258 and netropsin, and since the amides of these drugs bind to DNA replacing the spine of hydration in a minor groove, it is proposed that a repeat of SPKK binds to DNA in the minor groove using similar hydrogen bonds. Previous ArticleNext Article Volume 8Issue 31 March 1989In this issue RelatedDetailsLoading ..." @default.
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- W86385217 date "1989-03-01" @default.
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- W86385217 title "SPKK, a new nucleic acid-binding unit of protein found in histone." @default.
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- W86385217 doi "https://doi.org/10.1002/j.1460-2075.1989.tb03440.x" @default.
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