Cytosolic HSP90 and HSP70 are essential components of INF1‐mediated hypersensitive response and non‐host resistance to<i>Pseudomonas cichorii</i>in<i>Nicotiana benthamiana</i>

Kanzaki, Hiromitsu; Saitoh, Hiromasa; Ito, Akiko; Fujisawa, Shizuko; Kamoun, Sophien; Katou, Shinpei; Yoshioka, Hirofumi; Terauchi, Ryohei

doi:10.1046/j.1364-3703.2003.00186.x

Cited by 219 publications

(168 citation statements)

References 26 publications

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“…Among the mutants with defects in the salicylic acid (SA) signal transduction pathway, nonhost resistance was diminished in eds1 mutants and transgenic plants with the bacterial NahG gene relative to wild-type plants (Parker et al, 1996;Mellersh and Heath, 2003;Yun et al, 2003;Zimmerli et al, 2004). Using virus-induced gene silencing, the chaperone and chaperone-like proteins HSP70, HSP90, and SGT1, which are thought to stabilize resistance (R) proteins and act upstream of EDS1, were shown to contribute to nonhost resistance in Nicotiana benthamiana (Peart et al, 2002;Kanzaki et al, 2003). Mutants with defects in the ethylene/jasmonate (ET/ JA) signal transduction pathways exhibited wild-type levels of nonhost resistance in Arabidopsis thaliana, even though there is evidence from microarray studies that this pathway is preferentially induced after inoculation of plants with some inappropriate pathogens (Huitema et al, 2003;Zimmerli et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2006

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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.

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Section: Introductionmentioning

confidence: 99%

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

et al. 2006

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“…In animals, HSP70s exert activities in processes such as oncogenesis, neurodegenerative and autoimmune diseases and viral infections [20][21][22]. In plants, it was reported that HSP70 and HSP90 are essential components in the INF1-mediated hypersensitive response in Nicotiana benthamiana, and that they function upstream or independent of the MAPK cascade [23]. Moreover, various reports describe that HSP70 expression in plants is induced upon infection with pathogens [23][24][25][26], but more detailed analysis of HSP70 expression profiles during plant-pathogen interactions are scarce.…”

Section: Introductionmentioning

confidence: 99%

Characterization of a wheat HSP70 gene and its expression in response to stripe rust infection and abiotic stresses

et al. 2010

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Members of the family of 70-kD heat shock proteins (HSP70 s) play various stress-protective roles in plants. In this study, a wheat HSP70 gene was isolated from a suppression subtractive hybridization (SSH) cDNA library of wheat leaves infected by Puccinia striiformis f. sp. tritici. The gene, that was designated as TaHSC70, was predicted to encode a protein of 690 amino acids, with a molecular mass of 73.54 KDa and a pI of 5.01. Further analysis revealed the presence of a conserved signature that is characteristic for HSP70s and phylogenetic analysis demonstrated that TaHSC70 is a homolog of chloroplast HSP70s. TaHSC70 mRNA was present in leaves of both green and etiolated wheat seedlings and in stems and roots. The transcript level in roots was approximately threefold less than in leaves but light-dark treatment did not charge TaHSC70 expression. Following heat shock of wheat seedlings at 40°C, TaHSC70 expression increased in leaves of etiolated seedlings but remained stable at the same level in green seedlings. In addition, TaHSC70 was differentially expressed during an incompatible and compatible interaction with wheat-stripe rust, and there was a transient increase in expression upon treatment with methyl jasmonate (MeJA) treatment. Salicylic acid (SA), ethylene (ET) and abscisic acid (ABA) treatments had no influence on TaHSC70 expression. These results suggest that TaHSC70 plays a role in stress-related responses, and in defense responses elicited by infection with stripe rust fungus and does so via a JA-dependent signal transduction pathway.

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“…So far, genetic approaches have identified relatively few components required for R gene function in plants [5]. A highly conserved protein class, the heat-shock proteins, has now been added to the list and work on these proteins promises to provide fresh insights to the molecular mechanics of the pathogen recognition process [6][7][8][9].…”

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confidence: 99%

Plant Immunity: The Origami of Receptor Activation

Schulze-Lefert¹

2004

Current Biology

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Mutations in plant cytosolicOne of the HSP90.2 substitutions is equivalent to that creating a mutant form of yeast HSP90 that lacks the ATPase activity required for client turnover, yet retains the ability to dimerize. Paradoxically, an insertion allele of AtHSP90.2, presumably a null mutation, had no discernible effect on RPM1 function. Furthermore, the Athsp90.2 mutant alleles with ATP binding site substitutions revealed a baroque genetic condition known as 'non-allelic non-complementation'. In such cases, F 1 heterozygous products of a cross between plants bearing two unlinked recessive mutations are phenotypically similar to either homozygous single mutant. In this particular case, F 1 plants containing wild-type and mutant alleles of both RPM1 and HSP90.2 were susceptible to P. syringae expressing avrRpm1.Non-allelic non-complementation provides clear evidence for dosage-sensitivity, and also suggests close physical associations -either direct physical interaction between RPM1 and HSP90.2 or an association in the same complex. Indeed, co-immunoprecipitation of RPM1 and HSP90 from plant extracts supported the conclusion that the proteins associate in vivo, although it remains to be shown whether the interaction is really direct and preferentially involves HSP90.2 and/or any of the other three closely related cytosolic HSP90 isoforms. One way of rationalizing the findings invokes functional redundancy in the HSP90 family, which could prevent inactivation of RPM1 in the Athsp90.2 null mutant, whereas mutations of the HSP90.2 ATPase domain might prohibit functional redundancy by causing persistent, but non-productive, client binding.In this scenario, non-productive binding might force incompletely folded RPM1 to enter a default degradation pathway. Hubert et al.[7] thus concluded that HSP90.2 has a role in folding RPM1 into a stable conformation or a signalling competent RPM1-containing complex. Preliminary evidence for the latter was obtained by co-immunoprecipitation experiments involving the Arabidopsis RIN4 protein. RIN4 is another component essential for RPM1 function and is known to interact directly with both RPM1 and the cognate Pseudomonas effector AvrRpm1 on the cytoplasmic face of plant plasma membranes [2]. In co-immunoprecipitation experiments, RIN4 did not appear to interact with HSP90, suggesting the existence of at least two pools of RPM1. This may also indicate that HSP90 acts transiently in the assembly of an RPM1-containing

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Cytosolic HSP90 and HSP70 are essential components of INF1‐mediated hypersensitive response and non‐host resistance toPseudomonas cichoriiinNicotiana benthamiana

Cited by 219 publications

References 26 publications

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

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

Characterization of a wheat HSP70 gene and its expression in response to stripe rust infection and abiotic stresses

Plant Immunity: The Origami of Receptor Activation

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