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JXB Advance Access originally published online on March 3, 2003
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Journal of Experimental Botany, Vol. 54, No. 385, pp. 1175-1181, April 1, 2003
© 2003 Oxford University Press

Isolation of tobacco ubiquitin-conjugating enzyme cDNA in a yeast two-hybrid system with tobacco ERF3 as bait and its characterization of specific interaction

Received 15 July 2002; Accepted 17 December 2002

Tomotsugu Koyama1,2, Takashi Okada1, Sakihito Kitajima5,1, Masaru Ohme-Takagi3, Hideaki Shinshi4 and Fumihiko Sato6,1,2

1 Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan
2 Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto 606-8502, Japan
3 Gene Function Research Laboratory, National Institute of Advanced Industrial Science and Technology (AIST), Central 6, 1-1 Higashi, Tsukuba 305-0046, Japan
4 Institute of Molecular and Cell Biology, National Institute of Advanced Industrial Science and Technology (AIST), Central 6, 1-1 Higashi, Tsukuba 305-0046, Japan

5 Present address: Graduate School of Science and Technology, Kyoto Institute of Technology, Matsugasaki, Kyoto 606-8585, Japan.
6 To whom correspondence should be addressed at the Department of Plant Gene and Totipotency, Graduate School of Biostudies, Kyoto University, Kyoto 606-8502, Japan. Fax: +81 75 753 6398. E-mail: fumihiko{at}kais.kyoto-u.ac.jp
Abbreviations: EAR, ERF-associated amphiphilic repression; ERF, ethylene-responsive factor; GAL4AD, GAL4 activation domain; GAL4BD, GAL4 binding domain; LUC, luciferase; NLP, nitrilase-like protein; SD, synthetic dropout, UBC, ubiquitin-conjugating enzyme.

Tobacco ETHYLENE-RESPONSIVE FACTOR3 (ERF3) is a member of the ERF-domain transcription factors and has a transcriptional repressor activity, whereas other ERF proteins show activation activity. To understand the regulation of ERF3-repressor activity, protein(s) were screened which interact with ERF3 in a yeast two-hybrid system. A partial sequence (B8) of NtUBC2, a tobacco ubiquitin-conjugating enzyme was isolated. This B8 specifically interacted with ERF3 in the yeast two-hybrid system. Further analyses revealed that the region unique to ERF3 interacted with B8. The physiological functions of NtUBC2 and the stability of ERF3 are discussed in relation to the regulation of the repression activity of ERF3.

Key words: Degradation, ethylene responsive factor (ERF), repressor, transient assay, two-hybrid system, ubiquitin-conjugating enzyme (UBC).


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