The Tobacco mosaic virus Replicase Protein Disrupts the Localization and Function of Interacting Aux/IAA Proteins
Previously, we identified a correlation between the interaction of the Tobacco mosaic virus (TMV) 126/183-kDa replicase with the auxin response regulator indole acetic acid (IAA)26/PAP1 and the development of disease symptoms. In this study, the TMV replicase protein is shown to colocalize with IAA2...
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| Format: | Article |
| Language: | English |
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The American Phytopathological Society
2006-08-01
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| Series: | Molecular Plant-Microbe Interactions |
| Subjects: | |
| Online Access: | https://apsjournals.apsnet.org/doi/10.1094/MPMI-19-0864 |
| _version_ | 1811290129721982976 |
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| author | Meenu S. Padmanabhan Haiymanot Shiferaw James N. Culver |
| author_facet | Meenu S. Padmanabhan Haiymanot Shiferaw James N. Culver |
| author_sort | Meenu S. Padmanabhan |
| collection | DOAJ |
| description | Previously, we identified a correlation between the interaction of the Tobacco mosaic virus (TMV) 126/183-kDa replicase with the auxin response regulator indole acetic acid (IAA)26/PAP1 and the development of disease symptoms. In this study, the TMV replicase protein is shown to colocalize with IAA26 in the cytoplasm and prevent its accumulation within the nucleus. Furthermore, two additional auxin (Aux)/IAA family members, IAA27 and IAA18, were found to interact with the TMV replicase and displayed alterations in their cellular localization or accumulation that corresponded with their ability to interact with the TMV replicase. In contrast, the localization and accumulation of noninteracting Aux/IAA proteins were unaffected by the presence of the viral replicase. To investigate the effects of the replicase interaction on Aux/IAA function, transgenic plants expressing a proteolysis-resistant IAA26-P108H-green fluorescent protein (GFP) protein were created. Transgenic plants accumulating IAA26-P108H-GFP displayed an abnormal developmental phenotype that included severe stunting and leaf epinasty. However, TMV infection blocked the nuclear localization of IAA26-P108H-GFP and attenuated the developmental phenotype displayed by the transgenic plants. Combined, these findings suggest that TMV-induced disease symptoms can be attributed, in part, to the ability of the viral replicase protein to disrupt the localization and subsequent function of interacting Aux/IAA proteins. |
| first_indexed | 2024-04-13T04:07:31Z |
| format | Article |
| id | doaj.art-317435aff6de4ad188068cc4014ff299 |
| institution | Directory Open Access Journal |
| issn | 0894-0282 1943-7706 |
| language | English |
| last_indexed | 2024-04-13T04:07:31Z |
| publishDate | 2006-08-01 |
| publisher | The American Phytopathological Society |
| record_format | Article |
| series | Molecular Plant-Microbe Interactions |
| spelling | doaj.art-317435aff6de4ad188068cc4014ff2992022-12-22T03:03:11ZengThe American Phytopathological SocietyMolecular Plant-Microbe Interactions0894-02821943-77062006-08-0119886487310.1094/MPMI-19-0864The Tobacco mosaic virus Replicase Protein Disrupts the Localization and Function of Interacting Aux/IAA ProteinsMeenu S. PadmanabhanHaiymanot ShiferawJames N. CulverPreviously, we identified a correlation between the interaction of the Tobacco mosaic virus (TMV) 126/183-kDa replicase with the auxin response regulator indole acetic acid (IAA)26/PAP1 and the development of disease symptoms. In this study, the TMV replicase protein is shown to colocalize with IAA26 in the cytoplasm and prevent its accumulation within the nucleus. Furthermore, two additional auxin (Aux)/IAA family members, IAA27 and IAA18, were found to interact with the TMV replicase and displayed alterations in their cellular localization or accumulation that corresponded with their ability to interact with the TMV replicase. In contrast, the localization and accumulation of noninteracting Aux/IAA proteins were unaffected by the presence of the viral replicase. To investigate the effects of the replicase interaction on Aux/IAA function, transgenic plants expressing a proteolysis-resistant IAA26-P108H-green fluorescent protein (GFP) protein were created. Transgenic plants accumulating IAA26-P108H-GFP displayed an abnormal developmental phenotype that included severe stunting and leaf epinasty. However, TMV infection blocked the nuclear localization of IAA26-P108H-GFP and attenuated the developmental phenotype displayed by the transgenic plants. Combined, these findings suggest that TMV-induced disease symptoms can be attributed, in part, to the ability of the viral replicase protein to disrupt the localization and subsequent function of interacting Aux/IAA proteins.https://apsjournals.apsnet.org/doi/10.1094/MPMI-19-0864subcellular localizationvirus disease |
| spellingShingle | Meenu S. Padmanabhan Haiymanot Shiferaw James N. Culver The Tobacco mosaic virus Replicase Protein Disrupts the Localization and Function of Interacting Aux/IAA Proteins Molecular Plant-Microbe Interactions subcellular localization virus disease |
| title | The Tobacco mosaic virus Replicase Protein Disrupts the Localization and Function of Interacting Aux/IAA Proteins |
| title_full | The Tobacco mosaic virus Replicase Protein Disrupts the Localization and Function of Interacting Aux/IAA Proteins |
| title_fullStr | The Tobacco mosaic virus Replicase Protein Disrupts the Localization and Function of Interacting Aux/IAA Proteins |
| title_full_unstemmed | The Tobacco mosaic virus Replicase Protein Disrupts the Localization and Function of Interacting Aux/IAA Proteins |
| title_short | The Tobacco mosaic virus Replicase Protein Disrupts the Localization and Function of Interacting Aux/IAA Proteins |
| title_sort | tobacco mosaic virus replicase protein disrupts the localization and function of interacting aux iaa proteins |
| topic | subcellular localization virus disease |
| url | https://apsjournals.apsnet.org/doi/10.1094/MPMI-19-0864 |
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