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The HSV-1 immediate early (IE) protein ICP4 (alpha 4, IE175, Vmw175) is an oligomeric molecule which activates transcription of viral early genes, represses transcription of viral IE genes, and binds to specific sequences in certain viral promoters. The extent to which these functions are interrelated has not been fully established. We have expressed truncated portions of the ICP4 gene in E. coli as trpE fusion proteins. DNA-binding studies with these hybrid proteins revealed that ICP4 residues 262 to 490 are sufficient for sequence-specific DNA-binding. DNA-binding was not detected with polypeptides extending from residue 262 to 464 or from residue 306 to 490. Multiple bands of protein-DNA complexes observed in gel mobility shift assays indicate that residues 262 to 490 may also contribute to the oligomerization of ICP4.

Codons 262 to 490 from the herpes simplex virus ICP4 gene are sufficient to encode a sequence-specific DNA binding protein