arabidopsis cam binding protein cbp60g contributes to mamp-induced sa accumulation and is involved in disease resistance against pseudomonas syringae拟南芥凸轮结合蛋白cbp60g有助于mamp-induced sa积累和参与抗病性两.pdfVIP

Arabidopsis CaM Binding Protein CBP60g Contributes to MAMP-Induced SA Accumulation and Is Involved in Disease Resistance against Pseudomonas syringae 1 1 1,2 3 1 1 Lin Wang , Kenichi Tsuda , Masanao Sato , Jerry D. Cohen , Fumiaki Katagiri , Jane Glazebrook * 1 Department of Plant Biology, Microbial and Plant Genomics Institute, University of Minnesota, St. Paul, Minnesota, United States of America, 2 Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Meguro-ku, Tokyo, Japan, 3 Department of Horticultural Science, Microbial and Plant Genomics Institute, University of Minnesota, St. Paul, Minnesota, United States of America Abstract Salicylic acid (SA)-induced defense responses are important factors during effector triggered immunity and microbe- associated molecular pattern (MAMP)-induced immunity in plants. This article presents evidence that a member of the Arabidopsis CBP60 gene family, CBP60g, contributes to MAMP-triggered SA accumulation. CBP60g is inducible by both pathogen and MAMP treatments. Pseudomonas syringae growth is enhanced in cbp60g mutants. Expression profiles of a cbp60g mutant after MAMP treatment are similar to those of sid2 and pad4, suggesting a defect in SA signaling. Accordingly, cbp60g mutants accumulate less SA when treated with the MAMP flg22 or a P. syringae hrcC strain that activates MAMP signaling. MAMP-induced production of reactive oxygen species and callose deposition are unaffected in cbp60g mutants. CBP60g is a calmodulin-binding protein with a calmodulin-binding domain located near the N-terminus. Calmodulin binding is dependent on Ca2+. Mutations in CBP60g that abolish calm