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Plant and Cell Physiology Advance Access published online on July 18, 2006
Plant and Cell Physiology, doi:10.1093/pcp/pcj080
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© The Japanese Society of Plant Physiologists (JSPP); all rights reserved.
Received April 1, 2006
Accepted June 20, 2006

Regular Paper

Fluorescence cross-correlation analyses of molecular interaction between an Aux/IAA protein, MSG2/IAA19, and protein-protein interaction domains of auxin response factors of Arabidopsis expressed in HeLa cells

Hideki Muto 1, Issei Nagao 2, Taku Demura 3, Hiroo Fukuda 4, Masataka Kinjo 2, and Kotaro T. Yamamoto 1 *

1 Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo, 060-0810 Japan
2 Laboratory of Supramolecular Biophysics, Research Institute for Electronic Science, Hokkaido University, Sapporo, 060-0812 Japan
3 Plant Science Center, RIKEN, 1-7-22 Suehiro, Tsurumi-ku, Yokohama, 230-0043 Japan
4 Plant Science Center, RIKEN, 1-7-22 Suehiro, Tsurumi-ku, Yokohama, 230-0043 Japan; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Hongo, Tokyo, 113-0033 Japan

* To whom correspondence should be addressed.
Kotaro T. Yamamoto, E-mail: kty{at}sci.hokudai.ac.jp


  Abstract

Since auxin may elicit numerous developmental responses by the use of a combination of auxin response factors (ARFs) and their Aux/IAA repressors, it is important to determine interaction between the two protein families in a quantitative manner. We transiently expressed the C-terminal protein-protein interaction domains (CTDs) of Arabidopsis ARFs, MP/ARF5 and NPH4/ARF7, and MSG2/IAA19, fused to fluorescent proteins in HeLa cells, and determined their molecular interactions with fluorescence cross-correlation spectroscopy (FCCS). Almost complete association was found between MSG2 and MP-CTD and between MSG2 and NPH4-CTD. Approximately 20% association was found for MSG2 homodimers, NPH4-CTD homodimers and MP-CTD/NPH4-CTDs heterodimers. Homotypic binding of MP-CTD may be weaker than that of MSG2. MSG2 was localized in cytoplasmic compartments in HeLa cells whereas it was localized in the nuclei in plant cells. The fact that the heterotypic interaction between MSG2 and ARF-CTDs is stronger than each of the homotypic interactions appears to be the molecular basis for tight control of the transcriptional activity of ARFs by auxin. These results also show that FCCS is useful to examine protein-protein interactions especially for transcriptional regulators.

Keywords: Arabidopsis thaliana; Auxin response factor; Aux/IAA protein; Fluorescence cross-correlation spectroscopy; HeLa cell; Protein-protein interaction.
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