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Nucleic Acids Research, 2001, Vol. 29, No. 17 3685-3693
© 2001 Oxford University Press

Detection of in vivo protein interactions between Snf1-related kinase subunits with intron-tagged epitope-labelling in plants cells

Alejandro Ferrando, Zsuzsana Koncz-Kálmán, Rosa Farràs, Antonio Tiburcio1, Jeff Schell and Csaba Koncz*

Max-Planck Institut für Züchtungsforschung, Carl-von-Linné-Weg 10, D-50829 Köln, Germany and 1Unitat de Fisiologia Vegetal, Universitat de Barcelona, Diagonal 643, 08028 Barcelona, Spain

Plant orthologs of the yeast sucrose non-fermenting (Snf1) kinase and mammalian AMP-activated protein kinase (AMPK) represent an emerging class of important regulators of metabolic and stress signalling. The catalytic {alpha}-subunits of plant Snf1-related kinases (SnRKs) interact in the yeast two-hybrid system with different proteins that share conserved domains with the ß- and {gamma}-subunits of Snf1 and AMPKs. However, due to the lack of a robust technique allowing the detection of protein interactions in plant cells, it is unknown whether these proteins indeed occur in SnRK complexes in vivo. Here we describe a double-labelling technique, using intron-tagged hemagglutinin (HA) and c-Myc epitope sequences, which provides a simple tool for co-immunopurification of interacting proteins expressed in Agrobacterium-transformed Arabidopsis cells. This generally applicable plant protein interaction assay was used to demonstrate that AKINß2, a plant ortholog of conserved Snf1/AMPK ß-subunits, forms different complexes with the catalytic {alpha}-subunits of Arabidopsis SnRK protein kinases AKIN10 and AKIN11 in vivo.

* To whom correspondence should be addressed. Tel: +49 221 5062 230; Fax: +49 221 5062 213; Email: koncz{at}mpiz-koeln.mpg.de


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