Changes in subcellular localization reveal interactions between human cytomegalovirus terminase subunits

<p>Abstract</p> <p>Background</p> <p>During herpesvirus replication, terminase packages viral DNA into capsids. The subunits of herpes simplex virus terminase, UL15, UL28, and UL33, assemble in the cytoplasm prior to nuclear import of the complex.</p> <p>Met...

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Main Authors: Wang Jian Ben, Zhu Yali, McVoy Michael A, Parris Deborah S
Format: Article
Language:English
Published: BMC 2012-12-01
Series:Virology Journal
Subjects:
Online Access:http://www.virologyj.com/content/9/1/315
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spelling doaj-e2888336e9ca43e0b83486ace7ae5d212020-11-25T00:20:33ZengBMCVirology Journal1743-422X2012-12-019131510.1186/1743-422X-9-315Changes in subcellular localization reveal interactions between human cytomegalovirus terminase subunitsWang Jian BenZhu YaliMcVoy Michael AParris Deborah S<p>Abstract</p> <p>Background</p> <p>During herpesvirus replication, terminase packages viral DNA into capsids. The subunits of herpes simplex virus terminase, UL15, UL28, and UL33, assemble in the cytoplasm prior to nuclear import of the complex.</p> <p>Methods</p> <p>To detect similar interactions between human cytomegalovirus terminase subunits, the orthologous proteins UL89, UL56, and UL51 were expressed in HEK-293 T cells (via transfection) or insect cells (via baculovirus infection) and subcellular localizations were detected by cellular fractionation and confocal microscopy.</p> <p>Results</p> <p>In both cell types, UL56 and UL89 expressed alone were exclusively cytoplasmic, whereas UL51 was ~50% nuclear. Both UL89 and UL56 became ~50% nuclear when expressed together, as did UL56 when expressed with UL51. Nuclear localization of each protein was greatest when all three proteins were co-expressed.</p> <p>Conclusions</p> <p>These results support inclusion of UL51 as an HCMV terminase subunit and suggest that nuclear import of human cytomegalovirus terminase may involve nuclear import signals that form cooperatively upon subunit associations.</p> http://www.virologyj.com/content/9/1/315HerpesvirusCytomegalovirusTerminaseDNA packagingGenome maturation
collection DOAJ
language English
format Article
sources DOAJ
author Wang Jian Ben
Zhu Yali
McVoy Michael A
Parris Deborah S
spellingShingle Wang Jian Ben
Zhu Yali
McVoy Michael A
Parris Deborah S
Changes in subcellular localization reveal interactions between human cytomegalovirus terminase subunits
Virology Journal
Herpesvirus
Cytomegalovirus
Terminase
DNA packaging
Genome maturation
author_facet Wang Jian Ben
Zhu Yali
McVoy Michael A
Parris Deborah S
author_sort Wang Jian Ben
title Changes in subcellular localization reveal interactions between human cytomegalovirus terminase subunits
title_short Changes in subcellular localization reveal interactions between human cytomegalovirus terminase subunits
title_full Changes in subcellular localization reveal interactions between human cytomegalovirus terminase subunits
title_fullStr Changes in subcellular localization reveal interactions between human cytomegalovirus terminase subunits
title_full_unstemmed Changes in subcellular localization reveal interactions between human cytomegalovirus terminase subunits
title_sort changes in subcellular localization reveal interactions between human cytomegalovirus terminase subunits
publisher BMC
series Virology Journal
issn 1743-422X
publishDate 2012-12-01
description <p>Abstract</p> <p>Background</p> <p>During herpesvirus replication, terminase packages viral DNA into capsids. The subunits of herpes simplex virus terminase, UL15, UL28, and UL33, assemble in the cytoplasm prior to nuclear import of the complex.</p> <p>Methods</p> <p>To detect similar interactions between human cytomegalovirus terminase subunits, the orthologous proteins UL89, UL56, and UL51 were expressed in HEK-293 T cells (via transfection) or insect cells (via baculovirus infection) and subcellular localizations were detected by cellular fractionation and confocal microscopy.</p> <p>Results</p> <p>In both cell types, UL56 and UL89 expressed alone were exclusively cytoplasmic, whereas UL51 was ~50% nuclear. Both UL89 and UL56 became ~50% nuclear when expressed together, as did UL56 when expressed with UL51. Nuclear localization of each protein was greatest when all three proteins were co-expressed.</p> <p>Conclusions</p> <p>These results support inclusion of UL51 as an HCMV terminase subunit and suggest that nuclear import of human cytomegalovirus terminase may involve nuclear import signals that form cooperatively upon subunit associations.</p>
topic Herpesvirus
Cytomegalovirus
Terminase
DNA packaging
Genome maturation
url http://www.virologyj.com/content/9/1/315
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AT zhuyali changesinsubcellularlocalizationrevealinteractionsbetweenhumancytomegalovirusterminasesubunits
AT mcvoymichaela changesinsubcellularlocalizationrevealinteractionsbetweenhumancytomegalovirusterminasesubunits
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