PMR5, an acetylation protein at the intersection of pectin biosynthesis and defense against fungal pathogens

Chiniquy, Dawn; Underwood, William; Corwin, Jason; Ryan, Andrew; Szemenyei, Heidi; Lim, Candice C.; Stonebloom, Solomon H.; Birdseye, Devon S.; Vogel, John; Kliebenstein, Daniel; Scheller, Henrik V.; Somerville, Shauna

doi:10.1111/tpj.14497

Title: PMR5, an acetylation protein at the intersection of pectin biosynthesis and defense against fungal pathogens

Journal Article · Wed Aug 14 00:00:00 UTC 2019 · The Plant Journal

DOI: https://doi.org/10.1111/tpj.14497 · OSTI ID:1609109

^[1];

^[1]; Corwin, Jason ^[2]; Ryan, Andrew ^[1]; Szemenyei, Heidi ^[1]; Lim, Candice C. ^[1]; Stonebloom, Solomon H. ^[3]; Birdseye, Devon S. ^[3];

^[4]; Kliebenstein, Daniel ^[2];

^[5]; Somerville, Shauna ^[1]

Univ. of California, Berkeley, CA (United States); Energy Biosciences Inst., Berkeley, CA (United States)
Univ. of California, Davis, CA (United States)
Joint BioEnergy Inst., Emeryville, CA (United States)
Univ. of California, Berkeley, CA (United States); USDOE Joint Genome Institute (JGI), Walnut Creek, CA (United States)
Univ. of California, Berkeley, CA (United States); Joint BioEnergy Inst., Emeryville, CA (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)

Powdery mildew (Golovinomyces cichoracearum), one of the most prolific obligate biotrophic fungal pathogens worldwide, infects its host by penetrating the plant cell wall without activating the plant's innate immune system. The Arabidopsis mutant powdery mildew resistant 5 (pmr5) carries a mutation in a putative pectin acetyltransferase gene that confers enhanced resistance to powdery mildew. In this work, we show that heterologously expressed PMR5 protein transfers acetyl groups from [¹⁴C]-acetyl-CoA to oligogalacturonides. Through site-directed mutagenesis, we show that three amino acids within a highly conserved esterase domain in putative PMR5 orthologs are necessary for PMR5 function. A suppressor screen of mutagenized pmr5 seed selecting for increased powdery mildew susceptibility identified two previously characterized genes affecting the acetylation of plant cell wall polysaccharides, RWA2 and TBR. The rwa2 and tbr mutants also suppress powdery mildew disease resistance in pmr6, a mutant defective in a putative pectate lyase gene. Cell wall analysis of pmr5 and pmr6, and their rwa2 and tbr suppressor mutants, demonstrates minor shifts in cellulose and pectin composition. In direct contrast to their increased powdery mildew resistance, both pmr5 and pmr6 plants are highly susceptibile to multiple strains of the generalist necrotroph Botrytis cinerea, and have decreased camalexin production upon infection with B. cinerea. These results illustrate that cell wall composition is intimately connected to fungal disease resistance and outline a potential route for engineering powdery mildew resistance into susceptible crop species.

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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States); USDOE Bioenergy Research Centers (BRC) (United States). Joint BioEnergy Inst. (JBEI); USDOE Joint Genome Institute (JGI), Walnut Creek, CA (United States)

Sponsoring Organization:: Energy Biosciences Institute; National Science Foundation (NSF); USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1609109

Journal Information:: The Plant Journal, Journal Name: The Plant Journal Journal Issue: 5 Vol. 100; ISSN 0960-7412

Publisher:: Society for Experimental BiologyCopyright Statement

Country of Publication:: United States

Language:: English

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59 BASIC BIOLOGICAL SCIENCES
cell wall biochemistry
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fungal disease
host resistance
pectin acetylation
powdery mildew

Title: PMR5, an acetylation protein at the intersection of pectin biosynthesis and defense against fungal pathogens

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