Soybean NDR1‐like proteins bind pathogen effectors and regulate resistance signaling. Issue 2 (30th December 2013)
- Record Type:
- Journal Article
- Title:
- Soybean NDR1‐like proteins bind pathogen effectors and regulate resistance signaling. Issue 2 (30th December 2013)
- Main Title:
- Soybean NDR1‐like proteins bind pathogen effectors and regulate resistance signaling
- Authors:
- Selote, Devarshi
Shine, M. B.
Robin, Guillaume P.
Kachroo, Aardra - Abstract:
- <abstract abstract-type="main" id="nph12654-abs-0001"> <title>Summary</title> <p> <list id="nph12654-list-0001" list-type="bullet"> <list-item> <p>Nonrace specific disease resistance 1 (NDR1) is a conserved downstream regulator of resistance (R) protein‐derived signaling. We identified two NDR1‐like sequences (GmNDR1a, b) from soybean, and investigated their roles in <italic>R‐</italic>mediated resistance and pathogen effector detection.</p> </list-item> <list-item> <p>Silencing <italic>GmNDR1a</italic> and <italic>b</italic> in soybean shows that these genes are required for resistance derived from the <italic>Rpg1‐b</italic>, <italic> Rpg3</italic>, and <italic>Rpg4</italic> loci, against <italic>Pseudomonas syringae</italic> (<italic>Psg</italic>) expressing <italic>avrB</italic>, <italic> avrB2</italic> and <italic>avrD1</italic>, respectively. Immunoprecipitation assays show that the GmNDR1 proteins interact with the AvrB2 and AvrD1 <italic>Psg</italic> effectors. This correlates with the enhanced virulence of <italic>Psg avrB2</italic> and <italic>Psg avrD1</italic> in GmNDR1‐silenced <italic>rpg3 rpg4</italic> plants, even though these strains are not normally more virulent on plants lacking cognate <italic>R</italic> loci.</p> </list-item> <list-item> <p>The GmNDR1 proteins interact with GmRIN4 proteins, but not with AvrB, or its cognate R protein Rpg1‐b. However, the GmNDR1 proteins promote AvrB‐independent activation of Rpg1‐b when coexpressed with a phosphomimic<abstract abstract-type="main" id="nph12654-abs-0001"> <title>Summary</title> <p> <list id="nph12654-list-0001" list-type="bullet"> <list-item> <p>Nonrace specific disease resistance 1 (NDR1) is a conserved downstream regulator of resistance (R) protein‐derived signaling. We identified two NDR1‐like sequences (GmNDR1a, b) from soybean, and investigated their roles in <italic>R‐</italic>mediated resistance and pathogen effector detection.</p> </list-item> <list-item> <p>Silencing <italic>GmNDR1a</italic> and <italic>b</italic> in soybean shows that these genes are required for resistance derived from the <italic>Rpg1‐b</italic>, <italic> Rpg3</italic>, and <italic>Rpg4</italic> loci, against <italic>Pseudomonas syringae</italic> (<italic>Psg</italic>) expressing <italic>avrB</italic>, <italic> avrB2</italic> and <italic>avrD1</italic>, respectively. Immunoprecipitation assays show that the GmNDR1 proteins interact with the AvrB2 and AvrD1 <italic>Psg</italic> effectors. This correlates with the enhanced virulence of <italic>Psg avrB2</italic> and <italic>Psg avrD1</italic> in GmNDR1‐silenced <italic>rpg3 rpg4</italic> plants, even though these strains are not normally more virulent on plants lacking cognate <italic>R</italic> loci.</p> </list-item> <list-item> <p>The GmNDR1 proteins interact with GmRIN4 proteins, but not with AvrB, or its cognate R protein Rpg1‐b. However, the GmNDR1 proteins promote AvrB‐independent activation of Rpg1‐b when coexpressed with a phosphomimic derivative of GmRIN4b.</p> </list-item> <list-item> <p>The role of GmNDR1 proteins in Rpg1‐b activation, their direct interactions with AvrB2/AvrD1, and a putative role in the virulence activities of Avr effectors, provides the first experimental evidence in support of the proposed role for NDR1 in transducing extracellular pathogen‐derived signals.</p> </list-item> </list> </p> </abstract> … (more)
- Is Part Of:
- New phytologist. Volume 202:Issue 2(2014)
- Journal:
- New phytologist
- Issue:
- Volume 202:Issue 2(2014)
- Issue Display:
- Volume 202, Issue 2 (2014)
- Year:
- 2014
- Volume:
- 202
- Issue:
- 2
- Issue Sort Value:
- 2014-0202-0002-0000
- Page Start:
- 485
- Page End:
- 498
- Publication Date:
- 2013-12-30
- Subjects:
- Botany -- Periodicals
580 - Journal URLs:
- http://nph.onlinelibrary.wiley.com/hub/journal/10.1111/(ISSN)1469-8137/ ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/nph.12654 ↗
- Languages:
- English
- ISSNs:
- 0028-646X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6085.000000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 3137.xml