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Plant Physiology Preview Published on October 22, 2008; 10.1104/pp.108.130419
OPEN ACCESS ARTICLE
Received September 26, 2008 The Arabidopsis Calcium Sensor Calcineurin B-Like 3 Inhibits the 5'-Methylthioadenosine Nucleosidase in a Calcium-Dependent Manner
Department of Molecular Biology, Sejong University, Seoul 143-747, Korea; School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Korea * Corresponding author; email: knkim{at}sejong.ac.kr.
Calcineurin B-like (CBL) proteins represent a unique family of calcium sensors in plant cells. Sensing the calcium signals elicited by a variety of abiotic stresses, CBLs transmit the information to a group of serine/threonine protein kinases (CIPKs), which are currently known as sole targets of the CBL family. Here, we report that the CBL3 member of this family has a novel interaction partner in addition to the CIPK proteins. Extensive yeast two-hybrid screenings with CBL3 as bait identified an interesting Arabidopsis cDNA clone (named AtMTAN), which encodes a polypeptide similar to E.coli 5'-methylthioadenosine nucleosidase (EcMTAN). Deletion analyses showed that CBL3 utilizes the different structural modules to interact with its distinct target proteins, CIPKs and AtMTAN. In vitro and in vivo analyses verified that CBL3 and AtMTAN physically associate only in the presence of Ca2+. In addition, we empirically demonstrated that the AtMTAN protein indeed possesses the 5'-methylthioadenosine (MTA) nucleosidase activity, which can be inhibited specifically by Ca2+-bound CBL3. Overall, these findings suggest that the CBL family members can relay the calcium signals in more diverse ways than previously thought. We also discuss a possible mechanism by which the CBL3-mediated calcium signaling regulates the biosynthesis of ethylene and polyamines, which are involved in plant growth and development as well as various stress responses.
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