NUCLEAR-LOCALIZATION AND TRANSCRIPTIONAL ACTIVATION ACTIVITIES OF TRUNCATED VERSIONS OF THE IMMEDIATE-EARLY GENE-PRODUCT OF EQUINE HERPESVIRUS-1

The equine herpesvirus 1 (EHV-1) immediate-early (IE) gene product encodes a nuclear regulatory protein capable of negatively autoregulating its own promoter, transactivating representative EHV-1 early promoters, and acting in a concerted fashion with accessory EHV-1 regulatory factors to transactivate EHV-1 late promoters. To identify IE amino acid sequences involved in nuclear localization and to examine the contribution of C-terminal portions of the IE polypeptide to transactivation, vectors that express various carboxy-terminally truncated IE polypeptides were constructed. It is demonstrated that amino acids 963 through 970 of the 1,487-amino-acid IE protein are required for efficient localization of the truncated IE polypeptides to the nuclei of transfected cells. In addition, it is demonstrated that the first 970 amino acids of the IE gene product are sufficient to transactivate the EHV-1 thymidine kinase promoter to significant levels (i.e., approximately 40% of the level of wild-type activation).