A ubiquitin carboxyl extension protein secreted from a plant‐parasitic nematode Globodera rostochiensis is cleaved in planta to promote plant parasitism. (28th February 2013)
- Record Type:
- Journal Article
- Title:
- A ubiquitin carboxyl extension protein secreted from a plant‐parasitic nematode Globodera rostochiensis is cleaved in planta to promote plant parasitism. (28th February 2013)
- Main Title:
- A ubiquitin carboxyl extension protein secreted from a plant‐parasitic nematode Globodera rostochiensis is cleaved in planta to promote plant parasitism
- Authors:
- Chronis, Demosthenis
Chen, Shiyan
Lu, Shunwen
Hewezi, Tarek
Carpenter, Sara C.D.
Loria, Rosemary
Baum, Thomas J.
Wang, Xiaohong - Abstract:
- <abstract abstract-type="main" id="tpj12125-abs-0001"> <title>Summary</title> <p>Nematode effector proteins originating from esophageal gland cells play central roles in suppressing plant defenses and in formation of the plant feeding cells that are required for growth and development of cyst nematodes. A gene (<italic>GrUBCEP12</italic>) encoding a unique ubiquitin carboxyl extension protein (UBCEP) that consists of a signal peptide for secretion, a mono‐ubiquitin domain, and a 12 amino acid carboxyl extension protein (CEP12) domain was cloned from the potato cyst nematode <italic>Globodera rostochiensis</italic>. This <italic>GrUBCEP12</italic> gene was expressed exclusively within the nematode's dorsal esophageal gland cell, and was up‐regulated in the parasitic second‐stage juvenile, correlating with the time when feeding cell formation is initiated. We showed that specific <italic>GrUBCEP12</italic> knockdown via RNA interference reduced nematode parasitic success, and that over‐expression of the secreted Gr<sup>Δ</sup><sup>SP</sup>UBCEP12 protein in potato resulted in increased nematode susceptibility, providing direct evidence that this secreted effector is involved in plant parasitism. Using transient expression assays in <italic>Nicotiana benthamiana</italic>, we found that Gr<sup>Δ</sup><sup>SP</sup>UBCEP12 is processed into free ubiquitin and a CEP12 peptide (GrCEP12) <italic>in planta</italic>, and that GrCEP12 suppresses resistance gene‐mediated cell death. A<abstract abstract-type="main" id="tpj12125-abs-0001"> <title>Summary</title> <p>Nematode effector proteins originating from esophageal gland cells play central roles in suppressing plant defenses and in formation of the plant feeding cells that are required for growth and development of cyst nematodes. A gene (<italic>GrUBCEP12</italic>) encoding a unique ubiquitin carboxyl extension protein (UBCEP) that consists of a signal peptide for secretion, a mono‐ubiquitin domain, and a 12 amino acid carboxyl extension protein (CEP12) domain was cloned from the potato cyst nematode <italic>Globodera rostochiensis</italic>. This <italic>GrUBCEP12</italic> gene was expressed exclusively within the nematode's dorsal esophageal gland cell, and was up‐regulated in the parasitic second‐stage juvenile, correlating with the time when feeding cell formation is initiated. We showed that specific <italic>GrUBCEP12</italic> knockdown via RNA interference reduced nematode parasitic success, and that over‐expression of the secreted Gr<sup>Δ</sup><sup>SP</sup>UBCEP12 protein in potato resulted in increased nematode susceptibility, providing direct evidence that this secreted effector is involved in plant parasitism. Using transient expression assays in <italic>Nicotiana benthamiana</italic>, we found that Gr<sup>Δ</sup><sup>SP</sup>UBCEP12 is processed into free ubiquitin and a CEP12 peptide (GrCEP12) <italic>in planta</italic>, and that GrCEP12 suppresses resistance gene‐mediated cell death. A target search showed that expression of <italic>RPN2a</italic>, a gene encoding a subunit of the 26S proteasome, was dramatically suppressed in <italic>Gr</italic><sup><italic>Δ</italic></sup><sup><italic>SP</italic></sup><italic>UBCEP</italic><italic>12</italic> but not <italic>GrCEP12</italic> over‐expression plants when compared with control plants. Together, these results suggest that, when delivered into host plant cells, Gr<sup>Δ</sup><sup>SP</sup>UBCEP12 becomes two functional units, one acting to suppress plant immunity and the other potentially affecting the host 26S proteasome, to promote feeding cell formation.</p> </abstract> … (more)
- Is Part Of:
- Plant journal. Volume 74:Number 2(2013:Apr.)
- Journal:
- Plant journal
- Issue:
- Volume 74:Number 2(2013:Apr.)
- Issue Display:
- Volume 74, Issue 2 (2013)
- Year:
- 2013
- Volume:
- 74
- Issue:
- 2
- Issue Sort Value:
- 2013-0074-0002-0000
- Page Start:
- 185
- Page End:
- 196
- Publication Date:
- 2013-02-28
- Subjects:
- Plant molecular biology -- Periodicals
Plant cells and tissues -- Periodicals
Botany -- Periodicals
580 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-313X ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/tpj.12125 ↗
- Languages:
- English
- ISSNs:
- 0960-7412
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6519.200000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3511.xml