Loss of a Callose Synthase Results in Salicylic Acid-Dependent Disease Resistance

Nishimura, Marc T.; Stein, Mónica; Hou, Bi-Huei; Vogel, John P.; Edwards, H. H.; Somerville, Shauna

doi:10.1126/science.1086716

Cited by 613 publications

(669 citation statements)

References 16 publications

Supporting

Mentioning

623

Contrasting

Unclassified

Order By: Relevance

“…In such instances, the papilla may seal the wound in the epidermal cell wall caused by the penetration peg, thereby potentially enabling the fungus to avoid recognition by the plant's surveillance mechanism. Consistent with this interpretation is the finding that the pmr4 callose synthase mutant of Arabidopsis has no callose in the papilla matrix and is resistant rather than hypersusceptible to the host powdery mildew (Jacobs et al, 2003;Nishimura et al, 2003). It appears that the host fungus evades recognition by the plant's surveillance mechanism and/or that it is capable of deflecting or detoxifying the plant's defenses.…”

Section: The Plant Trafficking Apparatus In Host Vs Nonhost Responsesmentioning

confidence: 84%

The PEN1 Syntaxin Defines a Novel Cellular Compartment upon Fungal Attack and Is Required for the Timely Assembly of Papillae

Assaad

Qiu

Youngs

et al. 2004

MBoC

Self Cite

352

388

View full text Add to dashboard Cite

Attack by the host powdery mildew Erysiphe cichoracearum usually results in successful penetration and rapid proliferation of the fungus on Arabidopsis. By contrast, the nonhost barley powdery mildew Blumeria graminis f. sp. hordei (Bgh) typically fails to penetrate Arabidopsis epidermal cells. In both instances the plant secretes cell wall appositions or papillae beneath the penetration peg of the fungus. Genetic screens for mutations that result in increased penetration of Bgh on Arabidopsis have recently identified the PEN1 syntaxin. Here we examine the role of PEN1 and of its closest homologue, SYP122, identified as a syntaxin whose expression is responsive to infection. pen1 syp122 double mutants are both dwarfed and necrotic, suggesting that the two syntaxins have overlapping functions. Although syp122-1 and the cell wall mur mutants have considerably more pronounced primary cell wall defects than pen1 mutants, these have relatively subtle or no effects on penetration resistance. Upon fungal attack, PEN1 appears to be actively recruited to papillae, and there is a 2-h delay in papillae formation in the pen1-1 mutant. We conclude that SYP122 may have a general function in secretion, including a role in cell wall deposition. By contrast, PEN1 appears to have a basal function in secretion and a specialized defense-related function, being required for the polarized secretion events that give rise to papilla formation.

show abstract

Section: The Plant Trafficking Apparatus In Host Vs Nonhost Responsesmentioning

confidence: 84%

The PEN1 Syntaxin Defines a Novel Cellular Compartment upon Fungal Attack and Is Required for the Timely Assembly of Papillae

Assaad

Qiu

Youngs

et al. 2004

MBoC

Self Cite

352

388

View full text Add to dashboard Cite

show abstract

“…Apart from priming for SAdependent resistance, BABA also primes for a faster and stronger deposition of callose-rich papillae under the appressoria of pathogenic fungi and oomycetes. Recently, we found that the callose-deficient mutant pmr4-1 (Nishimura et al, 2003) is blocked in BABA-IR against P. cucumerina and A. brassicicola (Ton and Mauch-Mani, 2004;J. Ton, unpublished results), suggesting that the augmented callose deposition is important for BABA-IR against these fungi.…”

Section: Introductionmentioning

confidence: 89%

Dissecting the β-Aminobutyric Acid–Induced Priming Phenomenon in Arabidopsis

et al. 2005

View full text Add to dashboard Cite

Plants treated with the nonprotein amino acid β-aminobutyric acid (BABA) develop an enhanced capacity to resist biotic and abiotic stresses. This BABA-induced resistance (BABA-IR) is associated with an augmented capacity to express basal defense responses, a phenomenon known as priming. Based on the observation that high amounts of BABA induce sterility in Arabidopsis thaliana, a mutagenesis screen was performed to select mutants impaired in BABA-induced sterility (ibs). Here, we report the isolation and subsequent characterization of three T-DNA–tagged ibs mutants. Mutant ibs1 is affected in a cyclin-dependent kinase–like protein, and ibs2 is defective in AtSAC1b encoding a polyphosphoinositide phosphatase. Mutant ibs3 is affected in the regulation of the ABA1 gene encoding the abscisic acid (ABA) biosynthetic enzyme zeaxanthin epoxidase. To elucidate the function of the three IBS genes in plant resistance, the mutants were tested for BABA-IR against the bacterium Pseudomonas syringae pv tomato, the oomycete Hyaloperonospora parasitica, and BABA-induced tolerance to salt. All three ibs mutants were compromised in BABA-IR against H. parasitica, although to a different extent. Whereas ibs1 was reduced in priming for salicylate (SA)-dependent trailing necrosis, mutants ibs2 and ibs3 were affected in the priming for callose deposition. Only ibs1 failed to express BABA-IR against P. syringae, which coincided with a defect in priming for SA-inducible PR-1 gene expression. By contrast, ibs2 and ibs3 showed reduced BABA-induced tolerance to salt, which correlated with an affected priming for ABA-inducible gene expression. For all three ibs alleles, the defects in BABA-induced sterility and BABA-induced protection against P. syringae, H. parasitica, and salt could be confirmed in independent mutants. The data presented here introduce three novel regulatory genes involved in priming for different defense responses.

show abstract

“…Of the PDR genes, only three, including PEN3, changed expression after inoculation with pathogens (see Supplemental Table 3 online) (Nishimura et al, 2003). Although PDR4 was repressed after infection, PDR12 was induced, and its induction was dramatically enhanced in B. g. hordei-inoculated pen3-1 plants.…”

Section: Expression Profiling Of Pen3-1 Plantsmentioning

confidence: 99%

“…When the mutation did not lead to a change in a restriction site, we generated derived CAPS markers using the dCAPS web tool (Neff et al, 1998). The Etr1-1 (Hua and Meyerowitz, 1998), NahG (Morris et al, 2000), rar1-10 , sgt1b , coi1-1 (Xie et al, 1998), pad4-1 (Nishimura et al, 2003), and npr1-1 (Nishimura et al, 2003) primers have been described previously. See Supplemental Table 5 online for a listing of primers used in genotyping mutations.…”

Section: Double Mutant Constructionmentioning

confidence: 99%

ArabidopsisPEN3/PDR8, an ATP Binding Cassette Transporter, Contributes to Nonhost Resistance to Inappropriate Pathogens That Enter by Direct Penetration

et al. 2006

Self Cite

View full text Add to dashboard Cite

Arabidopsis thaliana is a host to the powdery mildew Erysiphe cichoracearum and nonhost to Blumeria graminis f. sp hordei, the powdery mildew pathogenic on barley (Hordeum vulgare). Screening for Arabidopsis mutants deficient in resistance to barley powdery mildew identified PENETRATION3 (PEN3). pen3 plants permitted both increased invasion into epidermal cells and initiation of hyphae by B. g. hordei, suggesting that PEN3 contributes to defenses at the cell wall and intracellularly. pen3 mutants were compromised in resistance to the necrotroph Plectosphaerella cucumerina and to two additional inappropriate biotrophs, pea powdery mildew (Erysiphe pisi) and potato late blight (Phytophthora infestans). Unexpectedly, pen3 mutants were resistant to E. cichoracearum. This resistance was salicylic acid–dependent and correlated with chlorotic patches. Consistent with this observation, salicylic acid pathway genes were hyperinduced in pen3 relative to the wild type. The phenotypes conferred by pen3 result from the loss of function of PLEIOTROPIC DRUG RESISTANCE8 (PDR8), a highly expressed putative ATP binding cassette transporter. PEN3/PDR8 tagged with green fluorescent protein localized to the plasma membrane in uninfected cells. In infected leaves, the protein concentrated at infection sites. PEN3/PDR8 may be involved in exporting toxic materials to attempted invasion sites, and intracellular accumulation of these toxins in pen3 may secondarily activate the salicylic acid pathway.

show abstract

Loss of a Callose Synthase Results in Salicylic Acid-Dependent Disease Resistance

Cited by 613 publications

References 16 publications

The PEN1 Syntaxin Defines a Novel Cellular Compartment upon Fungal Attack and Is Required for the Timely Assembly of Papillae

The PEN1 Syntaxin Defines a Novel Cellular Compartment upon Fungal Attack and Is Required for the Timely Assembly of Papillae

Dissecting the β-Aminobutyric Acid–Induced Priming Phenomenon in Arabidopsis

ArabidopsisPEN3/PDR8, an ATP Binding Cassette Transporter, Contributes to Nonhost Resistance to Inappropriate Pathogens That Enter by Direct Penetration

Contact Info

Product

Resources

About