Purification of a set of cellular polypeptides that bind to the purine-rich cis-regulatory element of herpes simplex virus immediate early genes.

K. L. LaMarco, S. L. McKnight

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Abstract

Expression of herpes simplex virus type 1 (HSV1) immediate early (IE) genes is activated by a polypeptide component of the mature virion termed viral protein 16 (VP16). Stimulation of IE expression by VP16 operates via two cis-regulatory sequences: TAATGARAT, and the purine-rich hexanucleotide sequence GCGGAA. VP16 does not bind directly to either of the IE cis-regulatory sequences. Rather, these elements appear to represent binding sites for host cell proteins. Herein, we report the purification of a host cell factor that binds to the GCGGAA motif. We show further that this factor is capable of binding in vitro to an oligomerized form of the hexanucleotide sequence GAAACG, which is common to a variety of virus- and interferon-inducible genes. The GAAACG repeats of interferon- and virus-inducible genes, and the GA-rich repeats of HSV1 IE genes confer similar functional properties when appended to the promoter of a heterologous gene. These observations raise the possibility that HSV1 may activate its IE genes in a manner that exploits one of the components used by mammalian cells to combat virus infection.

Original languageEnglish (US)
Pages (from-to)1372-1383
Number of pages12
JournalGenes & development
Volume3
Issue number9
DOIs
StatePublished - Sep 1989

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ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

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