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Animal: DNA Viruses |
Department of Clinical Chemistry and Transfusion Medicine, Institute of Laboratory Medicine, Göteborg University, Sahlgrenska University Hospital, S-413 45 Gothenburg, Sweden1
Author for correspondence: Lars Rymo. Fax +46 31 82 84 58. e-mail Lars.Rymo{at}clinchem.gu.se
Using a yeast two-hybrid screen of a B-cell cDNA library with an Epstein–Barr nuclear antigen 5 (EBNA5) molecule containing seven repeats of the W1W2 domain as bait, we have isolated the EBNA5-interacting protein HAX-1. HAX-1 has previously been shown to associate with HS1, a protein specifically expressed in cells of the haematopoietic lineage, and is thought to be involved in signal transduction in B-cells. Immunofluorescence experiments showed that HAX-1 co-localized with the hsp60 protein that is associated with the mitochondria in the cell cytoplasm. Pull down experiments with a fusion protein between glutathione S-transferase and the seven copy repeat EBNA5 synthesized in bacteria and in yeast cells confirmed that HAX-1 can interact with EBNA5 in vitro. Conventionally, EBNA5 is regarded as a nuclear protein. However, we show here that the smallest EBNA5 species, composed of the unique Y domain and only one copy of the W1W2 repeat domain, like HAX-1, co-localizes with the mitochondrial hsp60 protein in the B-cell cytoplasm. Furthermore, immunoprecipitation experiments demonstrate that the single repeat EBNA5 associates with HAX-1 in transfected B-lymphoblastoid cells.
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