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BAG-1, a novel Bcl-2-interacting protein, activates expression of human JC virus

Division of Basic Medical Sciences, Faculty of Medicine, Memorial University of Newfoundland, St John’s, Newfoundland, Canada¹

Author for correspondence: Laxminarayana R. Devireddy. Present address: Howard Hughes Medical Institute, University of Massachusetts Medical Center, 373 Plantation Street, Suite 309, Worcester, MA 01605, USA. Fax +1 508 856 5473. e-mail Laxminarayana.Devireddy{at}umassmed.edu

Transcription of the human polyomavirus JC virus (JCV) genome is regulated by cellular proteins and the large tumour (T) antigen. Earlier studies led to the identification of nuclear factor-1 (NF-1)-binding sites in the JCV enhancer by DNase I protection assays of extracts from retinoic acid (RA)-differentiated P19 embryonal carcinoma (EC) cells. In this study, a cDNA clone that encodes a protein capable of binding to the JCV NF-1 sites was isolated from an RA-differentiated EC cell cDNA library. Sequence analysis revealed that the cDNA isolated was identical to the previously described Bcl-2-interacting protein BAG-1 (Bcl-2-associated athano gene-1). Results from RNA studies indicated that BAG-1 is expressed in several cell types. Co-transfection of a recombinant BAG-1 expression plasmid with JCV promoters indicated that BAG-1 stimulates transcription of the JCV_E promoter and to a lesser extent the JCV_L promoter. Mutations in the NF-1 sites in the JCV_E promoter eliminated the activation by BAG-1. Thus, BAG-1 is a novel transcription factor that may play a role in JCV expression.

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