EL5, a rice N‐acetylchitooligosaccharide elicitor‐responsive RING‐H2 finger protein, is a ubiquitin ligase which functions in vitro in co‐operation with an elicitor‐responsive ubiquitin‐conjugating enzyme, OsUBC5b

EL5, a rice N‐acetylchitooligosaccharide elicitor‐responsive RING‐H2 finger protein, is a... EL5, a rice gene responsive to N‐acetylchitooligosaccharide elicitor, encodes a RING‐H2 finger protein with structural features common to the plant‐specific ATL family. We show that the fusion protein of EL5 with maltose binding protein (MBP) was polyubiquitinated by incubation with ubiquitin, ubiquitin‐activating enzyme (E1), and the Ubc4/5 subfamily of the ubiquitin‐conjugating enzyme (E2). EL5 possesses the activity to catalyse the transfer of ubiquitin to the MBP moiety, and the RING‐H2 finger motif of EL5 is necessary for this activity. Thus, we concluded that EL5 represents a ubiquitin ligase (E3). We also show that two rice E2s (OsUBC5a, OsUBC5b) of the Ubc4/5 subfamily function as E2 which catalyses EL5‐mediated ubiquitination, and OsUBC5b was induced by elicitor, as well as EL5. These results strongly suggest that EL5 and OsUBC5b have roles in plant defense response through the turnover of protein(s) via the ubiquitin/proteasome system. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Plant Journal Wiley

EL5, a rice N‐acetylchitooligosaccharide elicitor‐responsive RING‐H2 finger protein, is a ubiquitin ligase which functions in vitro in co‐operation with an elicitor‐responsive ubiquitin‐conjugating enzyme, OsUBC5b

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Publisher
Wiley
Copyright
Copyright © 2002 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0960-7412
eISSN
1365-313X
DOI
10.1046/j.1365-313X.2002.01299.x
Publisher site
See Article on Publisher Site

Abstract

EL5, a rice gene responsive to N‐acetylchitooligosaccharide elicitor, encodes a RING‐H2 finger protein with structural features common to the plant‐specific ATL family. We show that the fusion protein of EL5 with maltose binding protein (MBP) was polyubiquitinated by incubation with ubiquitin, ubiquitin‐activating enzyme (E1), and the Ubc4/5 subfamily of the ubiquitin‐conjugating enzyme (E2). EL5 possesses the activity to catalyse the transfer of ubiquitin to the MBP moiety, and the RING‐H2 finger motif of EL5 is necessary for this activity. Thus, we concluded that EL5 represents a ubiquitin ligase (E3). We also show that two rice E2s (OsUBC5a, OsUBC5b) of the Ubc4/5 subfamily function as E2 which catalyses EL5‐mediated ubiquitination, and OsUBC5b was induced by elicitor, as well as EL5. These results strongly suggest that EL5 and OsUBC5b have roles in plant defense response through the turnover of protein(s) via the ubiquitin/proteasome system.

Journal

The Plant JournalWiley

Published: May 1, 2002

Keywords: ; ; ; ; ;

References

  • Use of a reporter transgene to generate Arabidopsis mutants in ubiquitin‐dependent protein degradation
    Bachmair, A.; Becker, F.; Schell, J.
  • Ubiquitylation in plants: a post‐genomic look at a post‐translational modification
    Bachmair, A.; Novatchkova, M.; Potuschak, T.; Eisenhaber, F.
  • Chemoperception of microbial signals in plant cells
    Boller, T.
  • Cryptogein affects expression of α3, α6 and β1, 20S proteasome subunits encoding genes in tobacco
    Dahan, J.; Etienne, P.; Petitot, A.S.; Houot, V.; Blein, J.P.; Suty, L.
  • Induction of tcI7, a gene encoding a β‐subunit of proteasome, in tobacco plants treated with elicitins, salicylic acid or hydrogen peroxide
    Etienne, P.; Petitot, A.S.; Houot, V.; Blein, J.P.; Suty, L.
  • Ubiquitin‐dependent proteolytic pathway in wheat germ: isolation of multiple forms of ubiquitin‐activating enzyme, E1
    Hatfield, P.M.; Vierstra, R.D.
  • Ubiquitin‐dependent protein degradation
    Hochstrasser, M.
  • Identification of a high affinity binding protein for N‐acetylchitooligosaccharide elicitor in the plasma membrane of suspension‐cultured rice cells by affinity labeling
    Ito, Y.; Kaku, H.; Shibuya, N.
  • Localization and binding characteristics of a high‐affinity binding site for N‐acetylchitooligosaccharide elicitor in the plasma membrane from suspension‐cultured rice cells suggest a role as a receptor for the elicitor signal at the cell surface
    Shibuya, N.; Ebisu, N.; Kamada, Y.; Kaku, H.; Cohn, J.; Ito, Y.

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