Cargando…
The constitutive expression of Arabidopsis plasmodesmal-associated class 1 reversibly glycosylated polypeptide impairs plant development and virus spread
Arabidopsis class 1 reversibly glycosylated polypeptides ((C1)RGPs) were shown to be plasmodesmal-associated proteins. Transgenic tobacco (Nicotiana tabacum) plants constitutively expressing GFP tagged AtRGP2 under the control of the CaMV 35S promoter are stunted, have a rosette-like growth pattern,...
Autores principales: | , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2791124/ https://www.ncbi.nlm.nih.gov/pubmed/19887501 http://dx.doi.org/10.1093/jxb/erp301 |
_version_ | 1782175163241988096 |
---|---|
author | Zavaliev, Raul Sagi, Guy Gera, Abed Epel, Bernard L. |
author_facet | Zavaliev, Raul Sagi, Guy Gera, Abed Epel, Bernard L. |
author_sort | Zavaliev, Raul |
collection | PubMed |
description | Arabidopsis class 1 reversibly glycosylated polypeptides ((C1)RGPs) were shown to be plasmodesmal-associated proteins. Transgenic tobacco (Nicotiana tabacum) plants constitutively expressing GFP tagged AtRGP2 under the control of the CaMV 35S promoter are stunted, have a rosette-like growth pattern, and in source leaves exhibit strong chlorosis, increased photoassimilate retention and starch accumulation that results in elevated leaf specific fresh and dry weights. Basal callose levels around plasmodesmata (Pd) of leaf epidermal cells in transgenic plants are higher than in WT. Such a phenotype is characteristic of virus-infected plants and some transgenic plants expressing Pd-associated viral movement proteins (MP). The local spread of Tobacco mosaic virus (TMV) is inhibited in AtRGP2:GFP transgenics compared to WT. Taken together these observations suggest that overexpression of the AtRGP2:GFP leads to a reduction in Pd permeability to photoassimilate, thus lowering the normal rate of translocation from source leaves to sink organs. Such a reduction may also inhibit the local cell-to-cell spread of viruses in transgenic plants. The observed reduction in Pd permeability could be due to a partial Pd occlusion caused either by the accumulation of AtRGP2:GFP fusion in Pd, and/or by constriction of Pd by the excessive callose accumulation. |
format | Text |
id | pubmed-2791124 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-27911242009-12-10 The constitutive expression of Arabidopsis plasmodesmal-associated class 1 reversibly glycosylated polypeptide impairs plant development and virus spread Zavaliev, Raul Sagi, Guy Gera, Abed Epel, Bernard L. J Exp Bot Research Papers Arabidopsis class 1 reversibly glycosylated polypeptides ((C1)RGPs) were shown to be plasmodesmal-associated proteins. Transgenic tobacco (Nicotiana tabacum) plants constitutively expressing GFP tagged AtRGP2 under the control of the CaMV 35S promoter are stunted, have a rosette-like growth pattern, and in source leaves exhibit strong chlorosis, increased photoassimilate retention and starch accumulation that results in elevated leaf specific fresh and dry weights. Basal callose levels around plasmodesmata (Pd) of leaf epidermal cells in transgenic plants are higher than in WT. Such a phenotype is characteristic of virus-infected plants and some transgenic plants expressing Pd-associated viral movement proteins (MP). The local spread of Tobacco mosaic virus (TMV) is inhibited in AtRGP2:GFP transgenics compared to WT. Taken together these observations suggest that overexpression of the AtRGP2:GFP leads to a reduction in Pd permeability to photoassimilate, thus lowering the normal rate of translocation from source leaves to sink organs. Such a reduction may also inhibit the local cell-to-cell spread of viruses in transgenic plants. The observed reduction in Pd permeability could be due to a partial Pd occlusion caused either by the accumulation of AtRGP2:GFP fusion in Pd, and/or by constriction of Pd by the excessive callose accumulation. Oxford University Press 2010-01 2009-11-03 /pmc/articles/PMC2791124/ /pubmed/19887501 http://dx.doi.org/10.1093/jxb/erp301 Text en © 2009 The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details) |
spellingShingle | Research Papers Zavaliev, Raul Sagi, Guy Gera, Abed Epel, Bernard L. The constitutive expression of Arabidopsis plasmodesmal-associated class 1 reversibly glycosylated polypeptide impairs plant development and virus spread |
title | The constitutive expression of Arabidopsis plasmodesmal-associated class 1 reversibly glycosylated polypeptide impairs plant development and virus spread |
title_full | The constitutive expression of Arabidopsis plasmodesmal-associated class 1 reversibly glycosylated polypeptide impairs plant development and virus spread |
title_fullStr | The constitutive expression of Arabidopsis plasmodesmal-associated class 1 reversibly glycosylated polypeptide impairs plant development and virus spread |
title_full_unstemmed | The constitutive expression of Arabidopsis plasmodesmal-associated class 1 reversibly glycosylated polypeptide impairs plant development and virus spread |
title_short | The constitutive expression of Arabidopsis plasmodesmal-associated class 1 reversibly glycosylated polypeptide impairs plant development and virus spread |
title_sort | constitutive expression of arabidopsis plasmodesmal-associated class 1 reversibly glycosylated polypeptide impairs plant development and virus spread |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2791124/ https://www.ncbi.nlm.nih.gov/pubmed/19887501 http://dx.doi.org/10.1093/jxb/erp301 |
work_keys_str_mv | AT zavalievraul theconstitutiveexpressionofarabidopsisplasmodesmalassociatedclass1reversiblyglycosylatedpolypeptideimpairsplantdevelopmentandvirusspread AT sagiguy theconstitutiveexpressionofarabidopsisplasmodesmalassociatedclass1reversiblyglycosylatedpolypeptideimpairsplantdevelopmentandvirusspread AT geraabed theconstitutiveexpressionofarabidopsisplasmodesmalassociatedclass1reversiblyglycosylatedpolypeptideimpairsplantdevelopmentandvirusspread AT epelbernardl theconstitutiveexpressionofarabidopsisplasmodesmalassociatedclass1reversiblyglycosylatedpolypeptideimpairsplantdevelopmentandvirusspread AT zavalievraul constitutiveexpressionofarabidopsisplasmodesmalassociatedclass1reversiblyglycosylatedpolypeptideimpairsplantdevelopmentandvirusspread AT sagiguy constitutiveexpressionofarabidopsisplasmodesmalassociatedclass1reversiblyglycosylatedpolypeptideimpairsplantdevelopmentandvirusspread AT geraabed constitutiveexpressionofarabidopsisplasmodesmalassociatedclass1reversiblyglycosylatedpolypeptideimpairsplantdevelopmentandvirusspread AT epelbernardl constitutiveexpressionofarabidopsisplasmodesmalassociatedclass1reversiblyglycosylatedpolypeptideimpairsplantdevelopmentandvirusspread |