Abstract
The human cytomegalovirus (HCMV) UL34 proteins localize to the nucleus. We identified a 204-amino-acid region, amino acids 40 to 244, as required for nuclear retention. A highly conserved 12-amino-acid section, amino acids 198 to 210, was required for nuclear localization. Although the nuclear localization and retention signals of pUL34 overlap the domain required for DNA-binding activity, the two regions are separable by point mutations. Our results presented here identify the first example of an HCMV protein with separable nuclear localization and retention signals.
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