Microscopic Analysis of Severe Structural Rearrangements of the Plant Endoplasmic Reticulum and Golgi Caused by Overexpression of Poa semilatent virus Movement Protein
Cell-to-cell transport of plant viruses is mediated by virus-encoded movement proteins and occurs through plasmodesmata interconnecting neighboring cells in plant tissues. Three movement proteins coded by the “triple gene block” (TGB) and named TGBp1, TGBp2 and TGBp3 have distinct functions in viral...
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| Format: | Article |
| Language: | English |
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Wiley
2012-01-01
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| Series: | The Scientific World Journal |
| Online Access: | http://dx.doi.org/10.1100/2012/416076 |
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| author | Andrey G. Solovyev Joachim Schiemann Sergey Y. Morozov |
| author_facet | Andrey G. Solovyev Joachim Schiemann Sergey Y. Morozov |
| author_sort | Andrey G. Solovyev |
| collection | DOAJ |
| description | Cell-to-cell transport of plant viruses is mediated by virus-encoded movement proteins and occurs through plasmodesmata interconnecting neighboring cells in plant tissues. Three movement proteins coded by the “triple gene block” (TGB) and named TGBp1, TGBp2 and TGBp3 have distinct functions in viral transport. TGBp1 binds viral genomic RNAs to form ribonucleoprotein complexes representing the transport form of viral genome, while TGBp2 and TGBp3 are necessary for intracellular delivery of such complexes to plasmodesmata. Recently, it was revealed that overexpression of Potato virus X TGBp3 triggers the unfolded protein response mitigating the endoplasmic reticulum (ER) stress leading to cell death if this protein reaches high levels in the ER. Here we report microscopic studies of the influence of the Poa semilatent hordeivirus TGBp3 overexpressed in Nicotiana benthamiana epidermal cells by particle bombardment on cell endomembranes and demonstrate that the protein C-terminal transmembrane segment contains a determinant responsible for vesiculation and coalescence of the endoplasmic reticulum and Golgi presumably accompanying the ER stress that can be induced upon high-level TGBp3 expression. |
| format | Article |
| id | doaj-art-c682d9f6d8484a91bf6dd39a2ce47a02 |
| institution | Kabale University |
| issn | 1537-744X |
| language | English |
| publishDate | 2012-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | The Scientific World Journal |
| spelling | doaj-art-c682d9f6d8484a91bf6dd39a2ce47a022025-02-03T01:32:43ZengWileyThe Scientific World Journal1537-744X2012-01-01201210.1100/2012/416076416076Microscopic Analysis of Severe Structural Rearrangements of the Plant Endoplasmic Reticulum and Golgi Caused by Overexpression of Poa semilatent virus Movement ProteinAndrey G. Solovyev0Joachim Schiemann1Sergey Y. Morozov2A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, RussiaJulius Kühn Institute (JKI), Federal Research Centre for Cultivated Plants, Institute for Biosafety of Genetically Modified Plants, Erwin-Baur-Street 27, 06484 Quedlinburg, GermanyA. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, RussiaCell-to-cell transport of plant viruses is mediated by virus-encoded movement proteins and occurs through plasmodesmata interconnecting neighboring cells in plant tissues. Three movement proteins coded by the “triple gene block” (TGB) and named TGBp1, TGBp2 and TGBp3 have distinct functions in viral transport. TGBp1 binds viral genomic RNAs to form ribonucleoprotein complexes representing the transport form of viral genome, while TGBp2 and TGBp3 are necessary for intracellular delivery of such complexes to plasmodesmata. Recently, it was revealed that overexpression of Potato virus X TGBp3 triggers the unfolded protein response mitigating the endoplasmic reticulum (ER) stress leading to cell death if this protein reaches high levels in the ER. Here we report microscopic studies of the influence of the Poa semilatent hordeivirus TGBp3 overexpressed in Nicotiana benthamiana epidermal cells by particle bombardment on cell endomembranes and demonstrate that the protein C-terminal transmembrane segment contains a determinant responsible for vesiculation and coalescence of the endoplasmic reticulum and Golgi presumably accompanying the ER stress that can be induced upon high-level TGBp3 expression.http://dx.doi.org/10.1100/2012/416076 |
| spellingShingle | Andrey G. Solovyev Joachim Schiemann Sergey Y. Morozov Microscopic Analysis of Severe Structural Rearrangements of the Plant Endoplasmic Reticulum and Golgi Caused by Overexpression of Poa semilatent virus Movement Protein The Scientific World Journal |
| title | Microscopic Analysis of Severe Structural Rearrangements of the Plant Endoplasmic Reticulum and Golgi Caused by Overexpression of Poa semilatent virus Movement Protein |
| title_full | Microscopic Analysis of Severe Structural Rearrangements of the Plant Endoplasmic Reticulum and Golgi Caused by Overexpression of Poa semilatent virus Movement Protein |
| title_fullStr | Microscopic Analysis of Severe Structural Rearrangements of the Plant Endoplasmic Reticulum and Golgi Caused by Overexpression of Poa semilatent virus Movement Protein |
| title_full_unstemmed | Microscopic Analysis of Severe Structural Rearrangements of the Plant Endoplasmic Reticulum and Golgi Caused by Overexpression of Poa semilatent virus Movement Protein |
| title_short | Microscopic Analysis of Severe Structural Rearrangements of the Plant Endoplasmic Reticulum and Golgi Caused by Overexpression of Poa semilatent virus Movement Protein |
| title_sort | microscopic analysis of severe structural rearrangements of the plant endoplasmic reticulum and golgi caused by overexpression of poa semilatent virus movement protein |
| url | http://dx.doi.org/10.1100/2012/416076 |
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