TY - JOUR
T1 - A pea NTPase, PsAPY1, recognizes signal molecules from microorganisms
AU - Kiba, Akinori
AU - Toyoda, Kazuhiro
AU - Yoshioka, Kazuaki
AU - Tsujimura, Kami
AU - Takahashi, Hirotaka
AU - Ichinose, Yuki
AU - Takeda, Tadahiro
AU - Kato, Toshiaki
AU - Shiraishi, Tomonori
N1 - Funding Information:
Acknowledgments We are grateful to Prof. Yasuo Niwa, Shizuoka University, Shizuoka, Japan, for providing the sGFP (S65T) vector. This research was supported in part by Grants from the Japan Society for the Promotion of Science and by Special Funds for Promoting Science and Technology from the Japan Ministry of Education, Culture, Sports, Science, and Technology. A.K. is grateful for a Postdoctoral Fellowship from the Japan Society for the Promotion of Science. Financial support from Sankyo-Agro. Co., Ltd., Tokyo, Japan, is also acknowledged.
PY - 2006/8
Y1 - 2006/8
N2 - Apyrases (E.C.3.6.1.5; NTP-NDPases) are distributed in the cytosol, nuclei, cytoskeleton, and on the surface of plant cells. Some may play an important role in signal transduction from exogenous stimuli. We previously found a protein of ca. 55-kDa (CWP-55) in an ATPase-rich fraction from the pea cell wall bound to the elicitor and supprescins (suppressors of defense) from pea pathogen Mycosphaerella pinodes. We cloned the cDNA of CWP-55 that coincided with PsAPY1, one of two NTPase clones in a pea cDNA library. An analysis with a green fluorescent protein fusion protein indicated that PsAPY1 was distributed in the cell wall, nucleus, and cytoplasm. The recombinant PsAPY1 expressed in Escherichia coli had ATP-hydrolyzing activity responsive not only to the elicitor and supprescins from the pea pathogen but also to other elicitors such as a bacterial harpin, a yeast extract, and a synthetic glycopeptide. Biotinylated fungal signal molecules were bound to the recombinant PsAPY1 specifically. Resonant mirror detection confirmed such binding characteristics of PsAPY1. Based on these results, we discuss the role of cell-wall-bound NTPases in recognizing and responding to microorganisms on the cell wall surface.
AB - Apyrases (E.C.3.6.1.5; NTP-NDPases) are distributed in the cytosol, nuclei, cytoskeleton, and on the surface of plant cells. Some may play an important role in signal transduction from exogenous stimuli. We previously found a protein of ca. 55-kDa (CWP-55) in an ATPase-rich fraction from the pea cell wall bound to the elicitor and supprescins (suppressors of defense) from pea pathogen Mycosphaerella pinodes. We cloned the cDNA of CWP-55 that coincided with PsAPY1, one of two NTPase clones in a pea cDNA library. An analysis with a green fluorescent protein fusion protein indicated that PsAPY1 was distributed in the cell wall, nucleus, and cytoplasm. The recombinant PsAPY1 expressed in Escherichia coli had ATP-hydrolyzing activity responsive not only to the elicitor and supprescins from the pea pathogen but also to other elicitors such as a bacterial harpin, a yeast extract, and a synthetic glycopeptide. Biotinylated fungal signal molecules were bound to the recombinant PsAPY1 specifically. Resonant mirror detection confirmed such binding characteristics of PsAPY1. Based on these results, we discuss the role of cell-wall-bound NTPases in recognizing and responding to microorganisms on the cell wall surface.
KW - Binding protein
KW - Cell wall
KW - Elicitor
KW - NTPase
KW - Receptor
KW - Suppressor of defense
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U2 - 10.1007/s10327-006-0279-7
DO - 10.1007/s10327-006-0279-7
M3 - Article
AN - SCOPUS:33748098340
SN - 1345-2630
VL - 72
SP - 238
EP - 246
JO - Journal of General Plant Pathology
JF - Journal of General Plant Pathology
IS - 4
ER -