Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22.
The herpes simplex virus protein VP22 is a major phosphoprotein of infected cells. In this study, we identify two serine phosphorylation sites within VP22 and show that the N-terminal site is a substrate for casein kinase II, while the extreme C-terminal site is a substrate for another, as yet unide...
| Main Authors: | , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
1999
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| _version_ | 1797072108051759104 |
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| author | Elliott, G O'Reilly, D O'Hare, P |
| author_facet | Elliott, G O'Reilly, D O'Hare, P |
| author_sort | Elliott, G |
| collection | OXFORD |
| description | The herpes simplex virus protein VP22 is a major phosphoprotein of infected cells. In this study, we identify two serine phosphorylation sites within VP22 and show that the N-terminal site is a substrate for casein kinase II, while the extreme C-terminal site is a substrate for another, as yet unidentified, cellular kinase. Furthermore, we show that a mutant of VP22 which has both sites altered is unable to incorporate phosphate in vivo, confirming that there are no other phosphorylation sites within VP22. |
| first_indexed | 2024-03-06T23:02:53Z |
| format | Journal article |
| id | oxford-uuid:62c9661b-96a5-4e4e-9c6c-9efca2b9ac92 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T23:02:53Z |
| publishDate | 1999 |
| record_format | dspace |
| spelling | oxford-uuid:62c9661b-96a5-4e4e-9c6c-9efca2b9ac922022-03-26T18:08:29ZIdentification of phosphorylation sites within the herpes simplex virus tegument protein VP22.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:62c9661b-96a5-4e4e-9c6c-9efca2b9ac92EnglishSymplectic Elements at Oxford1999Elliott, GO'Reilly, DO'Hare, PThe herpes simplex virus protein VP22 is a major phosphoprotein of infected cells. In this study, we identify two serine phosphorylation sites within VP22 and show that the N-terminal site is a substrate for casein kinase II, while the extreme C-terminal site is a substrate for another, as yet unidentified, cellular kinase. Furthermore, we show that a mutant of VP22 which has both sites altered is unable to incorporate phosphate in vivo, confirming that there are no other phosphorylation sites within VP22. |
| spellingShingle | Elliott, G O'Reilly, D O'Hare, P Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22. |
| title | Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22. |
| title_full | Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22. |
| title_fullStr | Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22. |
| title_full_unstemmed | Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22. |
| title_short | Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22. |
| title_sort | identification of phosphorylation sites within the herpes simplex virus tegument protein vp22 |
| work_keys_str_mv | AT elliottg identificationofphosphorylationsiteswithintheherpessimplexvirustegumentproteinvp22 AT oreillyd identificationofphosphorylationsiteswithintheherpessimplexvirustegumentproteinvp22 AT oharep identificationofphosphorylationsiteswithintheherpessimplexvirustegumentproteinvp22 |