Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity
The movement protein (MP) TGBp1 of the potexvirus Potato virus X (PVX) is a multifunctional protein required for cell-to-cell movement within the host plant. Recent work on other plant viruses has indicated that MP phosphorylation by host kinases can regulate MP function. In this study, we demonstra...
Guardado en:
| Autores principales: | , , , |
|---|---|
| Formato: | JOUR |
| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_01681702_v137_n1_p16_Modena |
| Aporte de: |
| id |
todo:paper_01681702_v137_n1_p16_Modena |
|---|---|
| record_format |
dspace |
| spelling |
todo:paper_01681702_v137_n1_p16_Modena2023-10-03T15:06:09Z Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity Módena, N.A. Zelada, A.M. Conte, F. Mentaberry, A. CK2 Phosphorylation PVX Triple gene block Viral mobilization casein kinase II protein tgbp1 unclassified drug virus protein alpha chain article controlled study in vitro study nonhuman nucleotide sequence Potexvirus priority journal protein expression protein function protein phosphorylation tobacco viral plant disease virus infection Casein Kinase II Molecular Sequence Data Phosphorylation Potexvirus Recombinant Proteins Serine Tobacco Viral Proteins Virus Replication Nicotiana tabacum Potato virus X Potexvirus The movement protein (MP) TGBp1 of the potexvirus Potato virus X (PVX) is a multifunctional protein required for cell-to-cell movement within the host plant. Recent work on other plant viruses has indicated that MP phosphorylation by host kinases can regulate MP function. In this study, we demonstrate that recombinant and native TGBp1 are phosphorylated by Nicotiana tabacum extracts from both PVX-infected and non-infected leaves. The phosphorylation activity present in plant extracts has distinctive characteristics of casein kinase 2 (CK2): it is inhibited by heparin, stimulated by polylysine, and uses either ATP or GTP as phosphoryl donors. We also demonstrate that TGBp1 is efficiently phosphorylated by recombinant tobacco CK2 α subunit and by partially purified tobacco CK2. Phosphopeptide mass mapping reveals that TGBp1 is phosphorylated in Ser-165, which is localized within a CK2 consensus sequence. Our results strongly suggest that a N. tabacum kinase of the CK2 family is involved in TBGp1 phosphorylation during the course of viral infection. © 2008. Fil:Módena, N.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Zelada, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Mentaberry, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_01681702_v137_n1_p16_Modena |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
CK2 Phosphorylation PVX Triple gene block Viral mobilization casein kinase II protein tgbp1 unclassified drug virus protein alpha chain article controlled study in vitro study nonhuman nucleotide sequence Potexvirus priority journal protein expression protein function protein phosphorylation tobacco viral plant disease virus infection Casein Kinase II Molecular Sequence Data Phosphorylation Potexvirus Recombinant Proteins Serine Tobacco Viral Proteins Virus Replication Nicotiana tabacum Potato virus X Potexvirus |
| spellingShingle |
CK2 Phosphorylation PVX Triple gene block Viral mobilization casein kinase II protein tgbp1 unclassified drug virus protein alpha chain article controlled study in vitro study nonhuman nucleotide sequence Potexvirus priority journal protein expression protein function protein phosphorylation tobacco viral plant disease virus infection Casein Kinase II Molecular Sequence Data Phosphorylation Potexvirus Recombinant Proteins Serine Tobacco Viral Proteins Virus Replication Nicotiana tabacum Potato virus X Potexvirus Módena, N.A. Zelada, A.M. Conte, F. Mentaberry, A. Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity |
| topic_facet |
CK2 Phosphorylation PVX Triple gene block Viral mobilization casein kinase II protein tgbp1 unclassified drug virus protein alpha chain article controlled study in vitro study nonhuman nucleotide sequence Potexvirus priority journal protein expression protein function protein phosphorylation tobacco viral plant disease virus infection Casein Kinase II Molecular Sequence Data Phosphorylation Potexvirus Recombinant Proteins Serine Tobacco Viral Proteins Virus Replication Nicotiana tabacum Potato virus X Potexvirus |
| description |
The movement protein (MP) TGBp1 of the potexvirus Potato virus X (PVX) is a multifunctional protein required for cell-to-cell movement within the host plant. Recent work on other plant viruses has indicated that MP phosphorylation by host kinases can regulate MP function. In this study, we demonstrate that recombinant and native TGBp1 are phosphorylated by Nicotiana tabacum extracts from both PVX-infected and non-infected leaves. The phosphorylation activity present in plant extracts has distinctive characteristics of casein kinase 2 (CK2): it is inhibited by heparin, stimulated by polylysine, and uses either ATP or GTP as phosphoryl donors. We also demonstrate that TGBp1 is efficiently phosphorylated by recombinant tobacco CK2 α subunit and by partially purified tobacco CK2. Phosphopeptide mass mapping reveals that TGBp1 is phosphorylated in Ser-165, which is localized within a CK2 consensus sequence. Our results strongly suggest that a N. tabacum kinase of the CK2 family is involved in TBGp1 phosphorylation during the course of viral infection. © 2008. |
| format |
JOUR |
| author |
Módena, N.A. Zelada, A.M. Conte, F. Mentaberry, A. |
| author_facet |
Módena, N.A. Zelada, A.M. Conte, F. Mentaberry, A. |
| author_sort |
Módena, N.A. |
| title |
Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity |
| title_short |
Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity |
| title_full |
Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity |
| title_fullStr |
Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity |
| title_full_unstemmed |
Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity |
| title_sort |
phosphorylation of the tgbp1 movement protein of potato virus x by a nicotiana tabacum ck2-like activity |
| url |
http://hdl.handle.net/20.500.12110/paper_01681702_v137_n1_p16_Modena |
| work_keys_str_mv |
AT modenana phosphorylationofthetgbp1movementproteinofpotatovirusxbyanicotianatabacumck2likeactivity AT zeladaam phosphorylationofthetgbp1movementproteinofpotatovirusxbyanicotianatabacumck2likeactivity AT contef phosphorylationofthetgbp1movementproteinofpotatovirusxbyanicotianatabacumck2likeactivity AT mentaberrya phosphorylationofthetgbp1movementproteinofpotatovirusxbyanicotianatabacumck2likeactivity |
| _version_ |
1807315737848578048 |