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J. Biol. Chem., Vol. 279, Issue 2, 928-936, January 9, 2004

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Plant MAPK Phosphatase Interacts with Calmodulins^*

Hiromoto Yamakawa¶||, Shinpei Katou, Shigemi Seo, Ichiro Mitsuhara, Hiroshi Kamada¶, and Yuko Ohashi**

From the Plant Physiology Department, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki 305-8602, Japan, Program for Promotion of Basic Research Activities for Innovative Biosciences, Minato-ku, Tokyo 105-0001, Japan, and ^¶Institute of Biological Sciences, University of Tsukuba, Ibaraki 305-8572, Japan

A mitogen-activated protein kinase (MAPK) phosphatase gene, designated NtMKP1, was isolated as a candidate gene for a calmodulin (CaM)-binding protein from tobacco. NtMKP1 protein has four characteristic domains conserved among plant MAPK phosphatases reported so far, namely a dual specificity protein phosphatase catalytic domain, gelsolin-like domain, putative CaM-binding domain (CaMBD), and serine-rich region, indicating that NtMKP1 is the ortholog of Arabidopsis MKP1. The bacterially expressed NtMKP1 protein physically interacted with three plant-specific types of CaM in an overlay assay with labeled CaMs, showing high affinity to NtCaM1 and NtCaM3 but lower affinity to NtCaM13. The peptide for the putative CaMBD bound both NtCaM1 and NtCaM3 significantly but bound NtCaM13 only slightly. Moreover, CaM overlay assays with mutated CaMBDs revealed that Trp⁴⁴⁰ and Leu⁴⁴³ in the middle of the basic amphiphilic -helix motif (amino acids 436–453) are critical for binding CaM. In comparison with the transient accumulation of a wound-induced MAPK, WIPK transcript, a prolonged activation of NtMKP1 expression was found in response to wounding and tobacco mosaic virus-induced hypersensitive reaction. In transgenic tobacco plants overexpressing NtMKP1, wound-induced activation of SIPK, salicylic acid-induced MAPK, and WIPK was inhibited. These results suggest that plant CaMs are involved in these stress-activated MAPK cascades via NtMKP1.

Received for publication, September 16, 2003 , and in revised form, October 21, 2003.

^* This work was supported in part by grants from a Center of Excellence project and a grant-in-aid for scientific research on molecular mechanisms of plant-pathogenic microbe interaction from the Ministry of Education, Science and Culture of Japan and by a grant from the Japan Society for the Promotion of Science Research Fellowship for Young Scientists (to S. K.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBank^TM/EBI Data Bank with accession number(s) AB117525.

^|| Present address: National Agricultural Research Center, Tsukuba, Ibaraki 305-8666, Japan.

^** To whom correspondence should be addressed: Plant Physiology Dept., National Institute of Agrobiological Sciences, Kannondai 2-1-2, Tsukuba, Ibaraki 305-8602, Japan. Tel.: 81-29-838-7440; Fax: 81-29-838-7469; E-mail: yohashi{at}affrc.go.jp.

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