Identification of the interaction domain of the small terminase subunit pUL89 with the large subunit pUL56 of human cytomegalovirus.

@article{Thoma2006IdentificationOT,
  title={Identification of the interaction domain of the small terminase subunit pUL89 with the large subunit pUL56 of human cytomegalovirus.},
  author={Corina Thoma and Eva Maria Borst and Martin Messerle and Manuela Rieger and J. G. Hwang and Elke Bogner},
  journal={Biochemistry},
  year={2006},
  volume={45 29},
  pages={8855-63}
}
The small terminase subunit pUL89 of human cytomegalovirus (HCMV) is thought to be required for cleavage of viral DNA into unit-length genomes in the cleavage/packaging process. Immunoprecipitations with a UL89-specific antibody demonstrated that pUL89 occurs predominantly as a monomer of approximate M(r) 75.000 together with a dimer of approximate 150.000. This was confirmed by gel permeation chromatography. In view of its putative function, pUL89 needs to be transported into the nucleus. By… CONTINUE READING