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JXB Advance Access originally published online on October 3, 2008
Journal of Experimental Botany 2008 59(14):3997-4006; doi:10.1093/jxb/ern241
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© 2008 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

RESEARCH PAPER

Ethylene- and pathogen-inducible Arabidopsis acyl-CoA-binding protein 4 interacts with an ethylene-responsive element binding protein

Hong-Ye Li *, Shi Xiao * and Mee-Len Chye{dagger}

School of Biological Sciences, The University of Hong Kong, Pokfulam Road, Hong Kong, China

{dagger} To whom correspondence should be addressed: E-mail: mlchye{at}hkucc.hku.hk

Six genes encode proteins with acyl-CoA-binding domains in Arabidopsis thaliana. They are the small 10-kDa cytosolic acyl-CoA-binding protein (ACBP), membrane-associated ACBP1 and ACBP2, extracellularly-targeted ACBP3, and kelch-motif containing ACBP4 and ACBP5. Here, the interaction of ACBP4 with an A. thaliana ethylene-responsive element binding protein (AtEBP), identified in a yeast two-hybrid screen, was confirmed by co-immunoprecipitation. The subcellular localization of ACBP4 and AtEBP, was addressed using an ACBP4:DsRed red fluorescent protein fusion and a green fluorescent protein (GFP):AtEBP fusion. Transient expression of these autofluoresence-tagged proteins in agroinfiltrated tobacco leaves, followed by confocal laser scanning microscopy, indicated their co-localization predominantly at the cytosol which was confirmed by FRET analysis. Immuno-electron microscopy on Arabidopsis sections not only localized ACBP4 to the cytosol but also to the periphery of the nucleus upon closer examination, perhaps as a result of its interaction with AtEBP. Furthermore, the expression of ACBP4 and AtEBP in Northern blot analyses was induced by the ethylene precursor 1-aminocyclopropane-1-carboxylic acid, methyl jasmonate treatments, and Botrytis cinerea infection, suggesting that the interaction of ACBP4 and AtEBP may be related to AtEBP-mediated defence possibly via ethylene and/or jasmonate signalling.

Key words: Acyl-CoA-binding protein, ethylene, pathogen, protein–protein interaction

* These authors contributed equally to the manuscript.

Received 22 July 2008; Revised 29 August 2008 Accepted 1 September 2008


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