Association of the herpes simplex virus regulatory protein ICP4 with specific nucleotide sequences in DNA.
We report that the herpes simplex virus (HSV) transcription regulatory protein designated ICP4 is a component of a stable complex between protein and specific nucleotide sequences in double-stranded DNA formed by addition of exogenous DNA to either a crude extract obtained from HSV-1 infected cells or a partially purified preparation of native ICP4. DNA sites which are bound directly or indirectly to ICP4 have been designated ICP4/protein binding sites. Three independent ICP4/protein binding sites have been identified by DNAse footprinting; two are in the vector pBR322 and one is located approximately 100 nucleotides upstream from the HSV glycoprotein D mRNA cap site. Comparison of the nucleotide sequences in these three sites reveals several regions of homology. We propose that the sequence 5'-ATCGTCNNNNYCGRC-3' (N = any base; Y = pyrimidine; R = purine) forms an essential component of the ICP4/protein binding site.
D001483:Base Sequence; D004247:DNA / Q000378:metabolism; D004269:DNA, Bacterial / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D003852:Deoxyribonucleoproteins / Q000032:analysis; D017874:Immediate-Early Proteins; D010957:Plasmids; D018139:Simplexvirus / Q000235:genetics*; D014764:Viral Proteins / Q000378:metabolism*
D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D003852:Deoxyribonucleoproteins; D017874:Immediate-Early Proteins; D014764:Viral Proteins; C048925:herpes simplex virus, type 1 protein ICP4; D004247:DNA