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標題: Unusually strong positive cooperativity in binding of peptides to latent membrane protein-1 DNA fragments of the Epstein-Barr viral gene
作者: Yang, C.H.
Jeng, K.C.G.
Yang, W.H.
Chen, Y.L.
Hung, C.C.
Lin, J.W.
Chen, S.T.
Richardson, S.
Martin, C.R.H.
Waring, M.J.
Sheh, L.
關鍵字: cooperative effects;footprinting;gene fragments;molecular;recognition;peptides;minor-groove;nasopharyngeal carcinoma;taiwanese population;virus;variant;transformation;recognition;inhibition;daunomycin;motifs;cells
Project: Chembiochem
期刊/報告no:: Chembiochem, Volume 7, Issue 8, Page(s) 1187-1196.
The DNA-binding preferences of two oligopeptide amides, (His-Pro-Arg-Lys)(3)NH2 (HR-12) and (Ser-Pro-Arg-Lys)(3)NH2 (SP-12), have been examined by quantitative DNase 1 footprinting studies. Two different DNA fragments were investigated: a pair of 5'-P-32-labeled duplexes from PBR322 with one or other of the complementary strands labeled and a corresponding pair or 5'-P-32-labeled duplexes representing fragments of the latent membrane protein (LMP-1) gene from a pathogenic Epstein-Barr virus variant derived from nasopharyngeal carcinoma. The major objective was to examine molecular recognition and cooperative features associated with sequence-selective binding of synthetic peptides to the LMP-1 fragments. At various binding sites on the pBR322 fragments, Hill coefficients (n(H)) ranging from 1.9-2.2 were observed; these results indicate modest positive cooperativity between binding sites for both peptides. By contrast, unusually high values of n(H), ranging from 4.0-9.3, were observed at various binding sites on the LMP-1 fragments. Allosteric models can be constructed to interpret the observed cooperative interactions between different DNA recognition sites in the LMP-1 gene upon binding of the peptide ligands. It is noteworthy that these models feature a novel network of cooperativity interconnecting multiple DNA allosteric sites. The evidence of sequence selectivity and strong cooperativity discovered in this work may prove to be a general feature of peptide interactions with some nucleic acids.
ISSN: 1439-4227
DOI: 10.1002/cbic.200600083
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