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   <subfield code="a">A pea NTPase, PsAPY1, recognizes signal molecules from microorganisms</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Akinori Kiba, Kazuhiro Toyoda, Kazuaki Yoshioka, Kami Tsujimura, Hirotaka Takahashi, Yuki Ichinose, Tadahiro Takeda, Toshiaki Kato, Tomonori Shiraishi]</subfield>
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   <subfield code="a">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.</subfield>
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