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Interaction of the human cytomegalovirus uracil DNA glycosylase UL114 with the viral DNA polymerase catalytic subunit UL54

Interaction between human cytomegalovirus uracil DNA glycosylase (UL114) and the viral DNA polymerase accessory subunit (UL44) has been reported; however, no such association was found in proteomic studies of UL44-interacting proteins. Utilizing virus expressing FLAG-tagged UL114, nuclease-resistant...

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Autores principales: Strang, Blair L., Coen, Donald M.
Formato: Texto
Lenguaje:English
Publicado: Society for General Microbiology 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3052538/
https://www.ncbi.nlm.nih.gov/pubmed/20410316
http://dx.doi.org/10.1099/vir.0.022160-0
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author Strang, Blair L.
Coen, Donald M.
author_facet Strang, Blair L.
Coen, Donald M.
author_sort Strang, Blair L.
collection PubMed
description Interaction between human cytomegalovirus uracil DNA glycosylase (UL114) and the viral DNA polymerase accessory subunit (UL44) has been reported; however, no such association was found in proteomic studies of UL44-interacting proteins. Utilizing virus expressing FLAG-tagged UL114, nuclease-resistant association of UL44 and the DNA polymerase catalytic subunit UL54 with UL114 was observed by co-immunoprecipitation. Contrary to a previous report, we observed that UL114 was much less abundant than UL44. Interaction of UL114 with UL54, independent of the UL54 carboxyl terminus, but not with UL44 was detected in vitro. Our data are consistent with a direct UL114–UL54 interaction, and suggest that UL114 and UL54 act in concert during base excision repair of the viral genome.
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spelling pubmed-30525382011-08-01 Interaction of the human cytomegalovirus uracil DNA glycosylase UL114 with the viral DNA polymerase catalytic subunit UL54 Strang, Blair L. Coen, Donald M. J Gen Virol Animal Interaction between human cytomegalovirus uracil DNA glycosylase (UL114) and the viral DNA polymerase accessory subunit (UL44) has been reported; however, no such association was found in proteomic studies of UL44-interacting proteins. Utilizing virus expressing FLAG-tagged UL114, nuclease-resistant association of UL44 and the DNA polymerase catalytic subunit UL54 with UL114 was observed by co-immunoprecipitation. Contrary to a previous report, we observed that UL114 was much less abundant than UL44. Interaction of UL114 with UL54, independent of the UL54 carboxyl terminus, but not with UL44 was detected in vitro. Our data are consistent with a direct UL114–UL54 interaction, and suggest that UL114 and UL54 act in concert during base excision repair of the viral genome. Society for General Microbiology 2010-08 /pmc/articles/PMC3052538/ /pubmed/20410316 http://dx.doi.org/10.1099/vir.0.022160-0 Text en Copyright © 2010, SGM
spellingShingle Animal
Strang, Blair L.
Coen, Donald M.
Interaction of the human cytomegalovirus uracil DNA glycosylase UL114 with the viral DNA polymerase catalytic subunit UL54
title Interaction of the human cytomegalovirus uracil DNA glycosylase UL114 with the viral DNA polymerase catalytic subunit UL54
title_full Interaction of the human cytomegalovirus uracil DNA glycosylase UL114 with the viral DNA polymerase catalytic subunit UL54
title_fullStr Interaction of the human cytomegalovirus uracil DNA glycosylase UL114 with the viral DNA polymerase catalytic subunit UL54
title_full_unstemmed Interaction of the human cytomegalovirus uracil DNA glycosylase UL114 with the viral DNA polymerase catalytic subunit UL54
title_short Interaction of the human cytomegalovirus uracil DNA glycosylase UL114 with the viral DNA polymerase catalytic subunit UL54
title_sort interaction of the human cytomegalovirus uracil dna glycosylase ul114 with the viral dna polymerase catalytic subunit ul54
topic Animal
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3052538/
https://www.ncbi.nlm.nih.gov/pubmed/20410316
http://dx.doi.org/10.1099/vir.0.022160-0
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