Skip Navigation


Molecular Plant Advance Access originally published online on February 11, 2008
Molecular Plant 2008 1(2):380-387; doi:10.1093/mp/ssn004
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
1/2/380    most recent
ssn004v1
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 Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Voet-van-Vormizeele, J.
Right arrow Articles by Groth, G.
Right arrow Search for Related Content
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2008. Published by the Molecular Plant Shanghai Editorial Office in association with Oxford University Press on behalf of CSPP and IPPE, SIBS, CAS.

Ethylene Controls Autophosphorylation of the Histidine Kinase Domain in Ethylene Receptor ETR1

Jan Voet-van-Vormizeele and Georg Groth1

Heinrich-Heine-Universität, Biochemie der Pflanzen, Universitätsstr. 1, 40225 Düsseldorf, Germany

1 To whom correspondence should be addressed. E-mail: georg.groth{at}uni-duesseldorf.de, fax (49)-211-8113569.

Perception of the phytohormone ethylene is accomplished by a small family of integral membrane receptors. In Arabidopsis, five ethylene receptor proteins are known, including ethylene resistant 1 (ETR1). The hydrophobic amino-terminal domain of these receptors contains the ethylene-binding site while the carboxyl-terminal part consists of a histidine kinase domain and a response regulator domain, which are well known elements found in bacterial two-component signaling. The soluble membrane-extrinsic carboxyl-terminal part of the receptor, which is likely to play an important role in signal transduction, showed intrinsic kinase activity when expressed and purified on its own. However, a correlation between signal input and autokinase activity was not established in these studies, as receptors were missing the transmembrane amino-terminal sensor domain. Thus, it is still unclear whether autophosphorylation occurs in response to perception of the ethylene signal. Here, we report on autophosphorylation studies of purified full-length ETR1. Autokinase activity of the purified receptor is controlled by ethylene or by ethylene agonists like the {pi}-acceptor compound cyanide. In fact, both signal molecules were able to completely turn off the intrinsic kinase activity. Furthermore, the observed inhibition of autophosphorylation in ETR1 by both molecules could be prevented when the ethylene antagonist 1-methyl-cyclopropene (MCP) was applied.

Key Words: ethylene pathway • phytohormone receptor • membrane protein • two-component system • signal transduction • Arabidopsis thaliana


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.