Unusually Strong Positive Cooperativity in Binding of Peptides to Latent Membrane Protein‐1 DNA Fragments of the Epstein–Barr Viral Gene

  title={Unusually Strong Positive Cooperativity in Binding of Peptides to Latent Membrane Protein‐1 DNA Fragments of the Epstein–Barr Viral Gene},
  author={Chia-Hung Yang and Kee Ching G. Jeng and Wan-Hsu Yang and Yu-ling Chen and Chia-Chun Hung and Juey-Wen Lin and Shui-Tein Chen and Simon Richardson and Christopher R. H. Martin and Michael J. Waring and Leung Sheh},
The DNA‐binding preferences of two oligopeptide amides, (His‐Pro‐Arg‐Lys)3NH2 (HR‐12) and (Ser‐Pro‐Arg‐Lys)3NH2 (SP‐12), have been examined by quantitative DNase I footprinting studies. Two different DNA fragments were investigated: a pair of 5′‐32P‐labeled duplexes from pBR322 with one or other of the complementary strands labeled and a corresponding pair of 5′‐32P‐labeled duplexes representing fragments of the latent membrane protein (LMP‐1) gene from a pathogenic Epstein–Barr virus variant… 
Determination of Allosteric Effects and Interstrand Bidentate Interactions in DNA‐Peptide Molecular Recognition
The interconnection of DNA footprints of peptides HypKK-10 and the parent peptide PyPro-12 supports the proposal that interaction network cooperativity is preferred in DNA-peptide interactions between multiple recognition sites.
Novel DNA-peptide interaction networks.
Investigation of various fluorescent protein–DNA binding peptides for effectively visualizing large DNA molecules
This investigation provided HMG-tagged FP–DBP as the best DNA staining reagent in terms of fluorescence intensity, signal-to-noise ratio, and DNA binding affinity (Kd = 586 nM).
Enthalpy-driven nuclease-like activity and mechanism of peptide-chlorambucil conjugates.
The strongly enthalpy-driven binding of CLB-peptide conjugates to preferred loci in DNA furnishes the required proximity effect to generate the observed nuclease-like sequence-selective cleavage.
Energetic studies on DNA-peptide interaction in relation to the enthalpy-entropy compensation paradox.
It is concluded that the preservation of a rather narrowly-defined ΔG value is central to the EEC in DNA-peptide interactions, illuminating the universal EEC paradox commonly found in diverse biochemical reactions.


SPKK, a new nucleic acid‐binding unit of protein found in histone.
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  • Biology, Chemistry
    The EMBO journal
  • 1989
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
‘SPKK’ motifs prefer to bind to DNA at A/T‐rich sites.
It is demonstrated 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.
Site and sequence specificity of the daunomycin-DNA interaction.
The site and sequence specificity of the daunomycin-DNA interaction was examined by equilibrium binding methods, by deoxyribonuclease I footprinting studies, and by examination of the effect of the
The heptad repeat in the largest subunit of RNA polymerase II binds by intercalating into DNA
It is shown that the repeat does indeed bind DNA and present evidence that it does so by the intercalation of tyrosine residues and a model of the unit composed of two β-turns was made and compared with the structure of the drug Triostin A which is known to intercalate into DNA.
All three domains of the Epstein-Barr virus-encoded latent membrane protein LMP-1 are required for transformation of rat-1 fibroblasts
It is demonstrated that all three major domains of LMP-1 (N-terminal, transmembrane, and C-terminals) are required for the ability to transform Rat-1 cells in culture, as assayed by loss of contact inhibition.
Preferential binding to DNA sequences of peptides related to a novel XPRK motif.
Sequence-selective interaction of the minor-groove interstrand cross-linking agent SJG-136 with naked and cellular DNA: footprinting and enzyme inhibition studies.
Footprinting studies have confirmed that high-affinity adducts do form at 5'-G-GATC-C-3' sequences and that these can inhibit RNA polymerase in a sequence-selective manner and SJG-136 efficiently inhibits the action of restriction endonuclease BglII.
Epstein-Barr virus latent membrane protein 1 is essential for B-lymphocyte growth transformation.
  • K. Kaye, K. Izumi, E. Kieff
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1993
LMP1 is essential for EBV-mediated transformation of primary B lymphocytes, that the first 43 amino acids are critical for LMP1's function, and that codon 44-initiated L MP1 does not have a dominant negative effect on transformation.
Strong binding in the DNA minor groove by an aromatic diamidine with a shape that does not match the curvature of the groove.
The results from a broad array of methods indicate that this compound binds to the minor groove of AT DNA sequences, and the amidine groups at both ends of the ligand and the -NH groups on the linker are involved in extensive and dynamic H-bonds to the DNA bases.
Cloning and characterization of the latent membrane protein (LMP) of a specific Epstein-Barr virus variant derived from the nasopharyngeal carcinoma in the Taiwanese population.
A DNA fragment containing Epstein-Barr virus (EBV) terminal fragment sequence was obtained from a genomic library of nasopharyngeal carcinoma (NPC) and contained the gene encoding latent membrane protein (LMP), which had 95% homology with the LMP sequence of the B95-8 strain.