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,...

Descripción completa

Detalles Bibliográficos
Autores principales: Zavaliev, Raul, Sagi, Guy, Gera, Abed, Epel, Bernard L.
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