Pepino mosaic virus triple gene block protein 1 (TGBp1) interacts with and increases tomato catalase 1 activity to enhance virus accumulation. (20th June 2013)
- Record Type:
- Journal Article
- Title:
- Pepino mosaic virus triple gene block protein 1 (TGBp1) interacts with and increases tomato catalase 1 activity to enhance virus accumulation. (20th June 2013)
- Main Title:
- Pepino mosaic virus triple gene block protein 1 (TGBp1) interacts with and increases tomato catalase 1 activity to enhance virus accumulation
- Authors:
- Mathioudakis, Matthaios M.
Veiga, Rita S. L.
Canto, Tomas
Medina, Vicente
Mossialos, Dimitris
Makris, Antonios M.
Livieratos, Ioannis - Abstract:
- <abstract abstract-type="main"> <title>Summary</title> <p>Various plant factors are co‐opted by virus elements (RNA, proteins) and have been shown to act in pathways affecting virus accumulation and plant defence. Here, an interaction between <italic>Pepino mosaic virus</italic> (PepMV) triple gene block protein 1 (TGBp1; p26) and tomato catalase 1 (CAT1), a crucial enzyme in the decomposition of toxic hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>), was identified using the yeast two‐hybrid assay, and confirmed via an <italic>in vitro</italic> pull‐down assay and bimolecular fluorescent complementation (BiFC) <italic>in planta</italic>. Each protein was independently localized within loci in the cytoplasm and nuclei, sites at which their interaction had been visualized by BiFC. Following PepMV inoculation, CAT mRNA and protein levels in leaves were unaltered at 0, 3 and 6 days (locally) and 8 days (systemically) post‐inoculation; however, leaf extracts from the last two time points contained increased CAT activity and lower H<sub>2</sub>O<sub>2</sub> levels. Overexpression of PepMV p26 <italic>in vitro</italic> and <italic>in planta</italic> conferred the same effect, suggesting an additional involvement of TGBp1 in potexvirus pathogenesis. The accumulation of PepMV genomic and subgenomic RNAs and the expression of viral coat protein in noninoculated (systemic) leaves were reduced significantly in CAT‐silenced plants. It is postulated that, during PepMV infection, a p26–CAT1<abstract abstract-type="main"> <title>Summary</title> <p>Various plant factors are co‐opted by virus elements (RNA, proteins) and have been shown to act in pathways affecting virus accumulation and plant defence. Here, an interaction between <italic>Pepino mosaic virus</italic> (PepMV) triple gene block protein 1 (TGBp1; p26) and tomato catalase 1 (CAT1), a crucial enzyme in the decomposition of toxic hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>), was identified using the yeast two‐hybrid assay, and confirmed via an <italic>in vitro</italic> pull‐down assay and bimolecular fluorescent complementation (BiFC) <italic>in planta</italic>. Each protein was independently localized within loci in the cytoplasm and nuclei, sites at which their interaction had been visualized by BiFC. Following PepMV inoculation, CAT mRNA and protein levels in leaves were unaltered at 0, 3 and 6 days (locally) and 8 days (systemically) post‐inoculation; however, leaf extracts from the last two time points contained increased CAT activity and lower H<sub>2</sub>O<sub>2</sub> levels. Overexpression of PepMV p26 <italic>in vitro</italic> and <italic>in planta</italic> conferred the same effect, suggesting an additional involvement of TGBp1 in potexvirus pathogenesis. The accumulation of PepMV genomic and subgenomic RNAs and the expression of viral coat protein in noninoculated (systemic) leaves were reduced significantly in CAT‐silenced plants. It is postulated that, during PepMV infection, a p26–CAT1 interaction increases H<sub>2</sub>O<sub>2</sub> scavenging, thus acting as a negative regulator of plant defence mechanisms to promote PepMV infections.</p> </abstract> … (more)
- Is Part Of:
- Molecular plant pathology. Volume 14:Number 6(2013:Aug.)
- Journal:
- Molecular plant pathology
- Issue:
- Volume 14:Number 6(2013:Aug.)
- Issue Display:
- Volume 14, Issue 6 (2013)
- Year:
- 2013
- Volume:
- 14
- Issue:
- 6
- Issue Sort Value:
- 2013-0014-0006-0000
- Page Start:
- 589
- Page End:
- 601
- Publication Date:
- 2013-06-20
- Subjects:
- Plant diseases -- Molecular aspects -- Periodicals
Plant-pathogen relationships -- Molecular aspects -- Periodicals
571.936 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1364-3703/issues ↗
http://www.blackwell-synergy.com/member/institutions/issuelist.asp?journal=mpp ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/mpp.12034 ↗
- Languages:
- English
- ISSNs:
- 1464-6722
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5900.826100
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 3149.xml