title: Critical structural elements of the VP16 transcriptional activation domain.
abstract: Virion protein 16 (VP16) of herpes simplex virus type 1 contains an acidic transcriptional activation domain. Missense mutations within this domain have provided insights into the structural elements critical for its function. Net negative charge contributed to, but was not sufficient for, transcriptional activation by VP16. A putative amphipathic alpha helix did not appear to be an important structural component of the activation domain. A phenylalanine residue at position 442 was exquisitely sensitive to mutation. Transcriptional activators of several classes contain hydrophobic amino acids arranged in patterns resembling that of VP16. Therefore, the mechanism of transcriptional activation by VP16 and other proteins may involve both ionic and specific hydrophobic interactions with target molecules.
authors.affiliation: Department of Biochemistry, Michigan State University, East Lansing 48824-1319.
authors.forename: W D
authors.initials: WD
authors.lastname: Cress
authors.forename: S J
authors.initials: SJ
authors.lastname: Triezenberg
mesh_terms: D000595:Amino Acid Sequence; D017874:Immediate-Early Proteins; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D018139:Simplexvirus; D013329:Structure-Activity Relationship; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics / Q000494:pharmacology; D014158:Transcription, Genetic / Q000187:drug effects*; D014162:Transfection; D014764:Viral Proteins / Q000235:genetics*; D014771:Virion
chemical_list: C050678:IE1 protein, Human herpesvirus 1; D017874:Immediate-Early Proteins; D014157:Transcription Factors; D014764:Viral Proteins