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Potato mop-top virus co-opts the stress sensor HIPP26 for long-distance movement
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dc.contributor.author | Cowan, Graham H. | |
dc.contributor.author | Roberts, Alison G. | |
dc.contributor.author | Jones, Susan | |
dc.contributor.author | Kumar, Pankaj | |
dc.contributor.author | Kalyandurg, Pruthvi B. | |
dc.contributor.author | Gil, Jose F. | |
dc.contributor.author | Savenkov, Eugene I. | |
dc.contributor.author | Hemsley, Piers A. | |
dc.contributor.author | Torrance, Lesley | |
dc.date.accessioned | 2018-05-23T15:30:05Z | |
dc.date.available | 2018-05-23T15:30:05Z | |
dc.date.issued | 2018-03-06 | |
dc.identifier | 252216138 | |
dc.identifier | b32965c9-7c0b-48fa-9c24-ca48d40daa96 | |
dc.identifier | 29374107 | |
dc.identifier | 000426848300019 | |
dc.identifier | 85043979525 | |
dc.identifier.citation | Cowan , G H , Roberts , A G , Jones , S , Kumar , P , Kalyandurg , P B , Gil , J F , Savenkov , E I , Hemsley , P A & Torrance , L 2018 , ' Potato mop-top virus co-opts the stress sensor HIPP26 for long-distance movement ' , Plant Physiology , vol. 176 , no. 3 , pp. 2052-2070 . https://doi.org/10.1104/pp.17.01698 | en |
dc.identifier.issn | 0032-0889 | |
dc.identifier.uri | https://hdl.handle.net/10023/13503 | |
dc.description | The work of LT, GC, SJ and AR is funded by the Scottish Government’s Rural and Environmental Science and Analytical Services (RESAS) Division, PH by the BBSRC (grant BB/M024911/1) and The Royal Society and EIS by the Swedish Research Council Formas and the Carl Tryggers Foundation. | en |
dc.description.abstract | Virus movement proteins facilitate virus entry into the vascular system to initiate systemic infection. The potato mop-top virus (PMTV) movement protein, TGB1, is involved in long-distance movement of both viral ribonucleoprotein complexes and virions. Here, our analysis of TGB1 interactions with host Nicotiana benthamiana proteins revealed an interaction with a member of the heavy metal-associated isoprenylated plant protein family, HIPP26, which acts as a plasma membrane-to-nucleus signal during abiotic stress. We found that knockdown of NbHIPP26 expression inhibited virus long-distance movement but did not affect cell-to-cell movement. Drought and PMTV infection up-regulated NbHIPP26 gene expression, and PMTV infection protected plants from drought. In addition, NbHIPP26 promoter-reporter fusions revealed vascular tissue-specific expression. Mutational and biochemical analyses indicated that NbHIPP26 subcellular localization at the plasma membrane and plasmodesmata was mediated by lipidation (S-acylation and prenylation), as nonlipidated NbHIPP26 was predominantly in the nucleus. Notably, coexpression of NbHIPP26 with TGB1 resulted in a similar nuclear accumulation of NbHIPP26. TGB1 interacted with the carboxyl-terminal CVVM (prenyl) domain of NbHIPP26, and bimolecular fluorescence complementation revealed that the TGB1-HIPP26 complex localized to microtubules and accumulated in the nucleolus, with little signal at the plasma membrane or plasmodesmata. These data support a mechanism where interaction with TGB1 negates or reverses NbHIPP26 lipidation, thus releasing membrane-associated NbHIPP26 and redirecting it via microtubules to the nucleus, thereby activating the drought stress response and facilitating virus long-distance movement. | |
dc.format.extent | 19 | |
dc.format.extent | 647833 | |
dc.language.iso | eng | |
dc.relation.ispartof | Plant Physiology | en |
dc.subject | NAC transcription factors | en |
dc.subject | Nicotiana-benthamiana | en |
dc.subject | Nucleolar localization | en |
dc.subject | Plant transformation | en |
dc.subject | Functional-analysis | en |
dc.subject | Brassica-napus | en |
dc.subject | Small RNAs | en |
dc.subject | Protein | en |
dc.subject | Phloem | en |
dc.subject | Arabidopsis | en |
dc.subject | QH301 Biology | en |
dc.subject | QR355 Virology | en |
dc.subject | NDAS | en |
dc.subject | BDC | en |
dc.subject.lcc | QH301 | en |
dc.subject.lcc | QR355 | en |
dc.title | Potato mop-top virus co-opts the stress sensor HIPP26 for long-distance movement | en |
dc.type | Journal article | en |
dc.contributor.institution | University of St Andrews. School of Biology | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.identifier.doi | 10.1104/pp.17.01698 | |
dc.description.status | Peer reviewed | en |
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