Extracellular RNase activity in healthy and rust infected wheat leaves

Barna, B.; Ibenthal, W.-D.; Heitefuß, R.

doi:10.1016/0885-5765(89)90085-4

Cited by 32 publications

(18 citation statements)

References 26 publications

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“…Notably, LRR1 potentiates the RNase activity of PR10. RNase activity is thought to be essential for the resistance response to microbial pathogens (Barna et al, 1989;Lusso and Kuc, 1995;Galiana et al, 1997;Shivakumar et al, 2000;Park et al, 2004). In this study, LRR1 is also shown to be a potential stimulator of PR10 phosphorylation, which could lead to the activation of defense and HR-like cell death.…”

Section: Lrr1 Promotes the Ribonuclease Activity And Phosphorylation mentioning

confidence: 68%

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Requirement of the Cytosolic Interaction between PATHOGENESIS-RELATED PROTEIN10 and LEUCINE-RICH REPEAT PROTEIN1 for Cell Death and Defense Signaling in Pepper

2012

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Plants recruit innate immune receptors such as leucine-rich repeat (LRR) proteins to recognize pathogen attack and activate defense genes. Here, we identified the pepper (Capsicum annuum) pathogenesis-related protein10 (PR10) as a leucine-rich repeat protein1 (LRR1)-interacting partner. Bimolecular fluorescence complementation and coimmunoprecipitation assays confirmed the specific interaction between LRR1 and PR10 in planta. Avirulent Xanthomonas campestris pv vesicatoria infection induces PR10 expression associated with the hypersensitive cell death response. Transient expression of PR10 triggers hypersensitive cell death in pepper and Nicotiana benthamiana leaves, which is amplified by LRR1 coexpression as a positive regulator. LRR1 promotes the ribonuclease activity and phosphorylation of PR10, leading to enhanced cell death signaling. The LRR1-PR10 complex is formed in the cytoplasm, resulting in its secretion into the apoplastic space. Engineered nuclear confinement of both proteins revealed that the cytoplasmic localization of the PR10-LRR1 complex is essential for cell death-mediated defense signaling. PR10/LRR1 silencing in pepper compromises resistance to avirulent X. campestris pv vesicatoria infection. By contrast, PR10/LRR1 overexpression in Arabidopsis thaliana confers enhanced resistance to Pseudomonas syringae pv tomato and Hyaloperonospora arabidopsidis. Together, these results suggest that the cytosolic LRR-PR10 complex is responsible for cell death-mediated defense signaling.

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Section: Lrr1 Promotes the Ribonuclease Activity And Phosphorylation mentioning

confidence: 68%

“…RNase activity was determined according to the method of Barna et al (1989) with minor modifications. Yeast RNA (200 mg) mixed with PR10 and LRR1 (0.1 to ;5.0 mg) was incubated in 400 mL of 100 mM MES, pH 6.0, at 568C for 30 min.…”

Section: Rnase Activity Assaymentioning

confidence: 99%

Requirement of the Cytosolic Interaction between PATHOGENESIS-RELATED PROTEIN10 and LEUCINE-RICH REPEAT PROTEIN1 for Cell Death and Defense Signaling in Pepper

2012

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“…Based on the correlation between the high level of RNase activity in the pistil and the low susceptibility of this tissue to pathogens, it has been proposed that RNases could participate in the defense mechanisms of plants (Lee et al, 1992). An increase in extracellular RNase activity in rust-infected wheat leaves has been observed compared with control leaves (Barna et al, 1989). Lusso and Kuc (1995) have reported the increase of RNase activity in tobacco plants induced to SAR with TMV after challenge inoculation with vira1 and funga1 pathogens.…”

Section: Antibes Cedex Francementioning

confidence: 99%

RNase Activity Prevents the Growth of a Fungal Pathogen in Tobacco Leaves and Increases upon Induction of Systemic Acquired Resistance with Elicitin

et al. 1997

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The hypersensitive response and systemic acquired resistance (SAR) can be induced in tobacco (Nicotiana tabacum 1.) plants by cryptogein, an elicitin secreted by Pbytopbfbora crypfogea. Stem application of cryptogein leads to the establishment of acquired resistance to subsequent leaf infection with Pbytopbfbora parasitica var nicotianae, the agent of the tobacco black shank disease. We have studied early events that occur after the infection and show here that a tobacco gene encoding the extracellular S-like RNase NE is expressed in response to inoculation with the pathogenic fungus.Upon induction of SAR with cryptogein, the accumulation of NE transcripts coincided with a rapid induction of RNase activity and with the increase in the activity of at least two different extracellular RNases. Moreover, exogenous application of RNase activity in the extracellular space of leaves led to a reduction of the fungus development by up to 90%, independently of any cryptogein treatment and in the absence of apparent necrosis. These results indicate that the up-regulation of apoplastic RNase activity after inoculation could contribute to the control of fungal invasion in plants induced to SAR with cryptogein.

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“…Phip Vb destroys RNAs demonstrated by RNase activity gels using the method of Yen and Green [7], and by measuring the spe cific RNase activity of recombinant Phip Vb according to the procedure of Barna ct al. [8] with slight modifications. These RNase may have an important function in pollenstigma recognition, as shown for S-locus RNases in tobacco plants [9],…”

Section: The Biological Function Of Phlpvmentioning

confidence: 99%

Molecular Characterization of Timothy Grass Pollen Group V Allergens

Becker¹,

Bufe²,

Petersen³

et al. 1995

Int Arch Allergy Immunol

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Phl p V is the dominant allergen of timothy grass (Phleum pratense) with two isoforms having the apparent molecular weights of 38 (Phl p Va) and 32 kD (Phlp Vb) under Western blot conditions. Two-dimensional electrophoresis/immunoblotting reveals that each isoform is split into at least four isoallergens. Structural differences in the isoforms are shown by N-terminal sequencing (only 60% identity), by reaction patterns of monoclonal antibodies and, more convincingly, by enzymic degradation of purified isoforms followed by immunologic fingerprinting. These findings are confirmed by the deduced primary protein structure of cloned Phl p Va and Phlp Vb. Experiments with IgE – affinity-purified by immobilized recombinant allergens or their fragments – reveal identical epitopes and at least one different epitope between the isoforms. Furthermore, on Phlp Va we can localize different IgE-reactive epitopes at the C terminus as well as the N terminus. By probing serum from 11 patients on recombinant C- or N-terminal fragments, an individual reaction pattern was found. Testing the histamine liberation potency of the fragments, we found the N-terminal fragment of Phlp Va to be superior to that of the C-terminal fragment or the whole molecule. These results give insights into the variability of allergens, the individuality of human reaction patterns to epitopes and the alteration of allergenicity to higher or lower levels by fragmentation.

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Extracellular RNase activity in healthy and rust infected wheat leaves

Cited by 32 publications

References 26 publications

Requirement of the Cytosolic Interaction between PATHOGENESIS-RELATED PROTEIN10 and LEUCINE-RICH REPEAT PROTEIN1 for Cell Death and Defense Signaling in Pepper

Requirement of the Cytosolic Interaction between PATHOGENESIS-RELATED PROTEIN10 and LEUCINE-RICH REPEAT PROTEIN1 for Cell Death and Defense Signaling in Pepper

RNase Activity Prevents the Growth of a Fungal Pathogen in Tobacco Leaves and Increases upon Induction of Systemic Acquired Resistance with Elicitin

Molecular Characterization of Timothy Grass Pollen Group V Allergens

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