arabidopsis mks1 is involved in basal immunity and requires an intact n-terminal domain for proper function拟南芥mks1参与基础免疫和适当的函数需要一个完整的n端结构域.pdfVIP

arabidopsis mks1 is involved in basal immunity and requires an intact n-terminal domain for proper function拟南芥mks1参与基础免疫和适当的函数需要一个完整的n端结构域.pdf

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arabidopsis mks1 is involved in basal immunity and requires an intact n-terminal domain for proper function拟南芥mks1参与基础免疫和适当的函数需要一个完整的n端结构域

Arabidopsis MKS1 Is Involved in Basal Immunity and Requires an Intact N-terminal Domain for Proper Function ¤ ¨ Klaus Petersen, Jin-Long Qiu , Juri Lutje, Berthe Katrine Fiil, Sidsel Hansen, John Mundy, Morten Petersen* Department of Biology, University of Copenhagen, Copenhagen, Denmark Abstract Background: Innate immune signaling pathways in animals and plants are regulated by mitogen-activated protein kinase (MAPK) cascades. MAP kinase 4 (MPK4) functions downstream of innate immune receptors via a nuclear substrate MKS1 to regulate the activity of the WRKY33 transcription factor, which in turn controls the production of anti-microbial phytoalexins. Methodology/Principal Findings: We investigate the role of MKS1 in basal resistance and the importance of its N- and C- terminal domains for MKS1 function. We used the information that mks1 loss-of-function partially suppresses the mpk4 loss- of-function phenotype, and that transgenic expression of functional MKS1 in mpk4/mks1 double mutants reverted the mpk4 dwarf phenotype. Transformation of mks1/mpk4 with mutant versions of MKS1 constructs showed that a single amino acid substitution in a putative MAP kinase docking domain, MKS1-L32A, or a truncated MKS1 version unable to interact with WRKY33, were deficient in reverting the double mutant to the mpk4 phenotype. These results demonstrate functional requirement in MKS1 for the interaction with MPK4 and WRKY33. In addition, nuclear localization of MKS1 was shown to depend on an intact N-terminal domain. Furthermore, loss-of-function mks1 mutants exhibited increased susceptibility to strains of Pseudomonas syringae and Hyaloperonospora arabidopsidis, indicati

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