A duplicated pair of Arabidopsis RING‐finger E3 ligases contribute to the RPM1‐ and RPS2‐mediated hypersensitive response

A duplicated pair of Arabidopsis RING‐finger E3 ligases contribute to the RPM1‐ and... The Arabidopsis RPM1 protein confers resistance to disease caused by Pseudomonas syringae strains delivering either the AvrRpm1 or AvrB type III effector proteins into host cells. We characterized two closely related RPM1‐interacting proteins, RIN2 and RIN3. RIN2 and RIN3 encode RING‐finger type ubiquitin ligases with six apparent transmembrane domains and an ubiquitin‐binding CUE domain. RIN2 and RIN3 are orthologs of the mammalian autocrine motility factor receptor, a cytokine receptor localized in both plasma membrane caveolae and the endoplasmic reticulum. RIN2 is predominantly localized to the plasma membrane, as are RPM1 and RPS2. The C‐terminal regions of RIN2 and RIN3, including the CUE domain, interact strongly with an RPM1 N‐terminal fragment and weakly with a similar domain from the Arabidopsis RPS2 protein. RIN2 and RIN3 can dimerize through their C‐terminal regions. The RING‐finger domains of RIN2 and RIN3 encode ubiquitin ligases. Inoculation with P. syringae DC3000(avrRpm1) or P. syringae DC3000(avrRpt2) induces differential decreases of RIN2 mobility in SDS‐PAGE and disappearance of the majority of RIN2. A rin2 rin3 double mutant expresses diminished RPM1‐ and RPS2‐dependent hypersensitive response (HR), but no alteration of pathogen growth. Thus, the RIN2/RIN3 RING E3 ligases apparently act on a substrate that regulates RPM1‐ and RPS2‐dependent HR. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Plant Journal Wiley

A duplicated pair of Arabidopsis RING‐finger E3 ligases contribute to the RPM1‐ and RPS2‐mediated hypersensitive response

Loading next page...
 
/lp/wiley/a-duplicated-pair-of-arabidopsis-ring-finger-e3-ligases-contribute-to-kBqtqbTGmS
Publisher
Wiley
Copyright
Copyright © 2005 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0960-7412
eISSN
1365-313X
DOI
10.1111/j.1365-313X.2005.02525.x
Publisher site
See Article on Publisher Site

Abstract

The Arabidopsis RPM1 protein confers resistance to disease caused by Pseudomonas syringae strains delivering either the AvrRpm1 or AvrB type III effector proteins into host cells. We characterized two closely related RPM1‐interacting proteins, RIN2 and RIN3. RIN2 and RIN3 encode RING‐finger type ubiquitin ligases with six apparent transmembrane domains and an ubiquitin‐binding CUE domain. RIN2 and RIN3 are orthologs of the mammalian autocrine motility factor receptor, a cytokine receptor localized in both plasma membrane caveolae and the endoplasmic reticulum. RIN2 is predominantly localized to the plasma membrane, as are RPM1 and RPS2. The C‐terminal regions of RIN2 and RIN3, including the CUE domain, interact strongly with an RPM1 N‐terminal fragment and weakly with a similar domain from the Arabidopsis RPS2 protein. RIN2 and RIN3 can dimerize through their C‐terminal regions. The RING‐finger domains of RIN2 and RIN3 encode ubiquitin ligases. Inoculation with P. syringae DC3000(avrRpm1) or P. syringae DC3000(avrRpt2) induces differential decreases of RIN2 mobility in SDS‐PAGE and disappearance of the majority of RIN2. A rin2 rin3 double mutant expresses diminished RPM1‐ and RPS2‐dependent hypersensitive response (HR), but no alteration of pathogen growth. Thus, the RIN2/RIN3 RING E3 ligases apparently act on a substrate that regulates RPM1‐ and RPS2‐dependent HR.

Journal

The Plant JournalWiley

Published: Oct 1, 2005

Keywords: ; ; ; ;

References

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 18 million articles from more than
15,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Search

Query the DeepDyve database, plus search all of PubMed and Google Scholar seamlessly

Organize

Save any article or search result from DeepDyve, PubMed, and Google Scholar... all in one place.

Access

Get unlimited, online access to over 18 million full-text articles from more than 15,000 scientific journals.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve

Freelancer

DeepDyve

Pro

Price

FREE

$49/month
$360/year

Save searches from
Google Scholar,
PubMed

Create folders to
organize your research

Export folders, citations

Read DeepDyve articles

Abstract access only

Unlimited access to over
18 million full-text articles

Print

20 pages / month

PDF Discount

20% off