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Selective Interaction Between Chloroplast β-ATPase and TGB1(L88) Retards Severe Symptoms Caused by Alternanthera mosaic virus Infection
The multifunctional triple gene block protein 1 (TGB1) of the Potexvirus Alternanthera mosaic virus (AltMV) has been reported to have silencing suppressor, cell-to-cell movement, and helicase functions. Yeast two hybrid screening using an Arabidopsis thaliana cDNA library with TGB1 as bait, and co-p...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Korean Society of Plant Pathology
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4174830/ https://www.ncbi.nlm.nih.gov/pubmed/25288986 http://dx.doi.org/10.5423/PPJ.OA.09.2013.0097 |
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author | Seo, Eun-Young Nam, Jiryun Kim, Hyun-Seung Park, Young-Hwan Hong, Seok Myeong Lakshman, Dilip Bae, Hanhong Hammond, John Lim, Hyoun-Sub |
author_facet | Seo, Eun-Young Nam, Jiryun Kim, Hyun-Seung Park, Young-Hwan Hong, Seok Myeong Lakshman, Dilip Bae, Hanhong Hammond, John Lim, Hyoun-Sub |
author_sort | Seo, Eun-Young |
collection | PubMed |
description | The multifunctional triple gene block protein 1 (TGB1) of the Potexvirus Alternanthera mosaic virus (AltMV) has been reported to have silencing suppressor, cell-to-cell movement, and helicase functions. Yeast two hybrid screening using an Arabidopsis thaliana cDNA library with TGB1 as bait, and co-purification with TGB1 inclusion bodies identified several host proteins which interact with AltMV TGB1. Host protein interactions with TGB1 were confirmed by biomolecular fluorescence complementation, which showed positive TGB1 interaction with mitochondrial ATP synthase delta′ chain subunit (ATP synthase delta′), light harvesting chlorophyll-protein complex I subunit A4 (LHCA4), chlorophyll a/b binding protein 1 (LHB1B2), chloroplast-localized IscA-like protein (ATCPISCA), and chloroplast β-ATPase. However, chloroplast β-ATPase interacts only with TGB1(L88), and not with weak silencing suppressor TGB1(P88). This selective interaction indicates that chloroplast β-ATPase is not required for AltMV movement and replication; however, TRV silencing of chloroplast β-ATPase in Nicotiana benthamiana induced severe tissue necrosis when plants were infected by AltMV TGB1(L88) but not AltMV TGB1(P88), suggesting that β-ATPase selectively responded to TGB1(L88) to induce defense responses. |
format | Online Article Text |
id | pubmed-4174830 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Korean Society of Plant Pathology |
record_format | MEDLINE/PubMed |
spelling | pubmed-41748302014-10-06 Selective Interaction Between Chloroplast β-ATPase and TGB1(L88) Retards Severe Symptoms Caused by Alternanthera mosaic virus Infection Seo, Eun-Young Nam, Jiryun Kim, Hyun-Seung Park, Young-Hwan Hong, Seok Myeong Lakshman, Dilip Bae, Hanhong Hammond, John Lim, Hyoun-Sub Plant Pathol J Research Article The multifunctional triple gene block protein 1 (TGB1) of the Potexvirus Alternanthera mosaic virus (AltMV) has been reported to have silencing suppressor, cell-to-cell movement, and helicase functions. Yeast two hybrid screening using an Arabidopsis thaliana cDNA library with TGB1 as bait, and co-purification with TGB1 inclusion bodies identified several host proteins which interact with AltMV TGB1. Host protein interactions with TGB1 were confirmed by biomolecular fluorescence complementation, which showed positive TGB1 interaction with mitochondrial ATP synthase delta′ chain subunit (ATP synthase delta′), light harvesting chlorophyll-protein complex I subunit A4 (LHCA4), chlorophyll a/b binding protein 1 (LHB1B2), chloroplast-localized IscA-like protein (ATCPISCA), and chloroplast β-ATPase. However, chloroplast β-ATPase interacts only with TGB1(L88), and not with weak silencing suppressor TGB1(P88). This selective interaction indicates that chloroplast β-ATPase is not required for AltMV movement and replication; however, TRV silencing of chloroplast β-ATPase in Nicotiana benthamiana induced severe tissue necrosis when plants were infected by AltMV TGB1(L88) but not AltMV TGB1(P88), suggesting that β-ATPase selectively responded to TGB1(L88) to induce defense responses. Korean Society of Plant Pathology 2014-03 /pmc/articles/PMC4174830/ /pubmed/25288986 http://dx.doi.org/10.5423/PPJ.OA.09.2013.0097 Text en © The Korean Society of Plant Pathology This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Seo, Eun-Young Nam, Jiryun Kim, Hyun-Seung Park, Young-Hwan Hong, Seok Myeong Lakshman, Dilip Bae, Hanhong Hammond, John Lim, Hyoun-Sub Selective Interaction Between Chloroplast β-ATPase and TGB1(L88) Retards Severe Symptoms Caused by Alternanthera mosaic virus Infection |
title | Selective Interaction Between Chloroplast β-ATPase and TGB1(L88) Retards Severe Symptoms Caused by Alternanthera mosaic virus Infection |
title_full | Selective Interaction Between Chloroplast β-ATPase and TGB1(L88) Retards Severe Symptoms Caused by Alternanthera mosaic virus Infection |
title_fullStr | Selective Interaction Between Chloroplast β-ATPase and TGB1(L88) Retards Severe Symptoms Caused by Alternanthera mosaic virus Infection |
title_full_unstemmed | Selective Interaction Between Chloroplast β-ATPase and TGB1(L88) Retards Severe Symptoms Caused by Alternanthera mosaic virus Infection |
title_short | Selective Interaction Between Chloroplast β-ATPase and TGB1(L88) Retards Severe Symptoms Caused by Alternanthera mosaic virus Infection |
title_sort | selective interaction between chloroplast β-atpase and tgb1(l88) retards severe symptoms caused by alternanthera mosaic virus infection |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4174830/ https://www.ncbi.nlm.nih.gov/pubmed/25288986 http://dx.doi.org/10.5423/PPJ.OA.09.2013.0097 |
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