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      저자 : Jen Brady (검색결과 2 건)
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        Ser360 and Ser364 in the Kinase Domain of Tomato SlMAPKKKα are Critical for Programmed Cell Death Associated with Plant Immunity

        황인선,Jen Brady,Gregory B. Martin,오창식 한국식물병리학회 2017 Plant Pathology Journal Vol.33 No.2

        SlMAPKKKα, a tomato (Solanum lycopersicum)mitogen-activated protein kinase kinase kinase, is apositive regulator of Pto-mediated effector-triggeredimmunity, which elicits programmed cell death (PCD)in plants. In this study, we examined whether putativephosphorylation sites in the conserved activation segmentof the SlMAPKKKα kinase domain are criticalfor eliciting PCD. Three amino acids, threonine353,serine360 (Ser360), or serine364 (Ser364), in the conservedactivation segment of SlMAPKKKα kinase domainwere substituted to alanine (T353A, S360A, or S364A),and these variants were transiently expressed in tomatoand Nicotiana benthamiana plants. Two alaninesubstitutions, S360A and S364A, completely abolishedSlMAPKKKα PCD-eliciting activity in both plants,while T353A substitution did not affect its PCDelicitingactivity. SlMAPKKKα wild type and variantproteins accumulated to similar levels in plant leaves. However, SlMAPKKKα protein with the largest sizewas missed when either S360A or S364A substitutionswere expressed, whereas proteins with the smallermasses were more accumulated than those of fulllengthof SIMAPKKKα and T353A. These results suggestthat phosphorylation of SlMAPKKKα at Ser360and Ser364 is critical for PCD elicitation in plants.

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        Ser<sup>360</sup> and Ser<sup>364</sup> in the Kinase Domain of Tomato SIMAPKKKα are Critical for Programmed Cell Death Associated with Plant Immunity

        Hwang, In Sun,Brady, Jen,Martin, Gregory B.,Oh, Chang-Sik The Korean Society of Plant Pathology 2017 Plant Pathology Journal Vol.33 No.2

        $SIMAPKKK{\alpha}$, a tomato (Solanum lycopersicum) mitogen-activated protein kinase kinase kinase, is a positive regulator of Pto-mediated effector-triggered immunity, which elicits programmed cell death (PCD) in plants. In this study, we examined whether putative phosphorylation sites in the conserved activation segment of the $SIMAPKKK{\alpha}$ kinase domain are critical for eliciting PCD. Three amino acids, $threonine^{353}$, $serine^{360}$ ($Ser^{360}$), or $serine^{364}$ ($Ser^{364}$), in the conserved activation segment of $SIMAPKKK{\alpha}$ kinase domain were substituted to alanine (T353A, S360A, or S364A), and these variants were transiently expressed in tomato and Nicotiana benthamiana plants. Two alanine substitutions, S360A and S364A, completely abolished $SIMAPKKK{\alpha}$ PCD-eliciting activity in both plants, while T353A substitution did not affect its PCD-eliciting activity. $SIMAPKKK{\alpha}$ wild type and variant proteins accumulated to similar levels in plant leaves. However, $SIMAPKKK{\alpha}$ protein with the largest size was missed when either S360A or S364A substitutions were expressed, whereas proteins with the smaller masses were more accumulated than those of full-length of $SIMAPKKK{\alpha}$ and T353A. These results suggest that phosphorylation of $SIMAPKKK{\alpha}$ at $Ser^{360}$ and $Ser^{364}$ is critical for PCD elicitation in plants.

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