Plant Physiol.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

Plant Physiology Preview
Published on October 22, 2008; 10.1104/pp.108.130419

OPEN ACCESS ARTICLE
This Article
Free via Open Access: OA
Right arrow Full Text (Plant Physiology Preview (PDF))
Right arrow Supplemental Data
Right arrowOA All Versions of this Article:
148/4/1883    most recent
pp.108.130419v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Oh, S.-I.
Right arrow Articles by Kim, K.-N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Oh, S.-I.
Right arrow Articles by Kim, K.-N.
Agricola
Right arrow Articles by Oh, S.-I.
Right arrow Articles by Kim, K.-N.

Received September 26, 2008
Accepted October 16, 2008

The Arabidopsis Calcium Sensor Calcineurin B-Like 3 Inhibits the 5'-Methylthioadenosine Nucleosidase in a Calcium-Dependent Manner

Seung-Ick Oh , Jimyeong Park , Sunhee Yoon , Yungyeong Kim , Soojin Park , Migyeong Ryu , Min Jung Nam , Sung Han Ok , Jeong-Kook Kim , Jeong-Sheop Shin , and Kyung-Nam Kim *

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.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 2008 by the American Society of Plant Biologists