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RAR1 Positively Controls Steady State Levels of Barley MLA Resistance Proteins and Enables Sufficient MLA6 Accumulation for Effective Resistance

Stéphane Bieri, Stefan Mauch, Qian-Hua Shen, Jack Peart, Alessandra Devoto, Catarina Casais, Francesca Ceron, Sabine Schulze, Hans-Henning Steinbiß, Ken Shirasu, Paul Schulze-Lefert
Stéphane Bieri
Max-Planck-Institut für Züchtungsforschung, Department of Plant Microbe Interactions, D-50829 Köln, Germany
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Stefan Mauch
Max-Planck-Institut für Züchtungsforschung, Department of Plant Microbe Interactions, D-50829 Köln, Germany
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Qian-Hua Shen
Max-Planck-Institut für Züchtungsforschung, Department of Plant Microbe Interactions, D-50829 Köln, Germany
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Jack Peart
Sainsbury Laboratory, John Innes Centre, NR4 7UH Norwich, United Kingdom
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Alessandra Devoto
School of Biological Sciences, University of East Anglia, Norwich, NR4 7TJ, United Kingdom
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Catarina Casais
Sainsbury Laboratory, John Innes Centre, NR4 7UH Norwich, United Kingdom
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Francesca Ceron
Max-Planck-Institut für Züchtungsforschung, Department of Plant Microbe Interactions, D-50829 Köln, Germany
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Sabine Schulze
Max-Planck-Institut für Züchtungsforschung, Department of Plant Microbe Interactions, D-50829 Köln, Germany
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Hans-Henning Steinbiß
Max-Planck-Institut für Züchtungsforschung, Department of Plant Microbe Interactions, D-50829 Köln, Germany
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Ken Shirasu
Sainsbury Laboratory, John Innes Centre, NR4 7UH Norwich, United Kingdom
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Paul Schulze-Lefert
Max-Planck-Institut für Züchtungsforschung, Department of Plant Microbe Interactions, D-50829 Köln, Germany
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Published December 2004. DOI: https://doi.org/10.1105/tpc.104.026682

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Abstract

The polymorphic barley (Hordeum vulgare) Mla locus harbors allelic race-specific resistance (R) genes to the powdery mildew fungus Blumeria graminis f sp hordei. The highly sequence-related MLA proteins contain an N-terminal coiled-coil structure, a central nucleotide binding (NB) site, a Leu-rich repeat (LRR) region, and a C-terminal non-LRR region. Using transgenic barley lines expressing epitope-tagged MLA1 and MLA6 derivatives driven by native regulatory sequences, we show a reversible and salt concentration–dependent distribution of the intracellular MLA proteins in soluble and membrane-associated pools. A posttranscriptional process directs fourfold greater accumulation of MLA1 over MLA6. Unexpectedly, in rar1 mutant plants that are compromised for MLA6 but not MLA1 resistance, the steady state level of both MLA isoforms is reduced. Furthermore, differential steady state levels of MLA1/MLA6 hybrid proteins correlate with their requirement for RAR1; the RAR1-independent hybrid protein accumulates to higher levels and the RAR1-dependent one to lower levels. Interestingly, yeast two-hybrid studies reveal that the LRR domains of RAR1-independent but not RAR1-dependent MLA isoforms interact with SGT1, a RAR1 interacting protein required for the function of many NB-LRR type R proteins. Our findings implicate the existence of a conserved mechanism to reach minimal NB-LRR R protein thresholds that are needed to trigger effective resistance responses.

  • Received August 6, 2004.
  • Accepted October 4, 2004.
  • Published November 17, 2004.
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RAR1 Positively Controls Steady State Levels of Barley MLA Resistance Proteins and Enables Sufficient MLA6 Accumulation for Effective Resistance
Stéphane Bieri, Stefan Mauch, Qian-Hua Shen, Jack Peart, Alessandra Devoto, Catarina Casais, Francesca Ceron, Sabine Schulze, Hans-Henning Steinbiß, Ken Shirasu, Paul Schulze-Lefert
The Plant Cell Dec 2004, 16 (12) 3480-3495; DOI: 10.1105/tpc.104.026682

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RAR1 Positively Controls Steady State Levels of Barley MLA Resistance Proteins and Enables Sufficient MLA6 Accumulation for Effective Resistance
Stéphane Bieri, Stefan Mauch, Qian-Hua Shen, Jack Peart, Alessandra Devoto, Catarina Casais, Francesca Ceron, Sabine Schulze, Hans-Henning Steinbiß, Ken Shirasu, Paul Schulze-Lefert
The Plant Cell Dec 2004, 16 (12) 3480-3495; DOI: 10.1105/tpc.104.026682
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The Plant Cell Online: 16 (12)
The Plant Cell
Vol. 16, Issue 12
Dec 2004
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