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In situ Subcellular Fractionation of Adherent and Non-adherent Mammalian Cells
Published on: July 23, 2010
Changes in subcellular localization reveal interactions between human cytomegalovirus terminase subunits
Jian Ben Wang1, Yali Zhu, Michael A McVoy
1Department of Pediatrics, Virginia Commonwealth University, Richmond, VA 23298-0163, USA.
Virology Journal
|December 25, 2012
Summary
Human cytomegalovirus (HCMV) terminase subunits UL89, UL56, and UL51 interactions were studied. Co-expression promotes nuclear import, suggesting cooperative signals for HCMV terminase assembly.
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- Herpesvirus replication involves terminase complex packaging viral DNA into capsids.
- Herpes simplex virus terminase subunits (UL15, UL28, UL33) assemble in the cytoplasm before nuclear import.
Purpose of the Study:
- To investigate interactions between human cytomegalovirus (HCMV) terminase subunits.
- To determine the subcellular localization and assembly of HCMV terminase components.
Main Methods:
- Orthologous HCMV proteins UL89, UL56, and UL51 were expressed in HEK-293T and insect cells.
- Subcellular localization was analyzed using cellular fractionation and confocal microscopy.
Main Results:
- Individually, UL56 and UL89 were cytoplasmic; UL51 was partially nuclear.
- Co-expression of UL89 and UL56, or UL56 and UL51, resulted in partial nuclear localization.
- All three subunits (UL89, UL56, UL51) co-expressed showed maximal nuclear localization.
Conclusions:
- UL51 is likely a subunit of the HCMV terminase complex.
- Nuclear import of HCMV terminase may depend on cooperative formation of nuclear import signals upon subunit association.
