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A Nitrilase-Like Protein Interacts with GCC Box DNA-Binding Proteins Involved in Ethylene and Defense Responses1

Ping Xu2, Meena L. Narasimhan2, Teresa Samson, Maria A. Coca, Gyung-Hye Huh, Jianmin Zhou3, Gregory B. Martin, Paul M. Hasegawa, and Ray A. Bressan*

Center for Plant Environmental Stress Physiology, 1165 Horticulture Building, Purdue University, West Lafayette, Indiana 47907-1165 (P.X., M.L.N., T.S., M.A.C., G.-H.H., P.M.H., R.A.B.); and Department of Agronomy, Lilly Hall of Life Sciences, Purdue University, West Lafayette, Indiana 47907-1150 (J.Z., G.B.M.)

Ethylene-responsive element-binding proteins (EREBPs) of tobacco (Nicotiana tabacum L.) bind to the GCC box of many pathogenesis-related (PR) gene promoters, including osmotin (PR-5). The two GCC boxes on the osmotin promoter are known to be required, but not sufficient, for maximal ethylene responsiveness. EREBPs participate in the signal transduction pathway leading from exogenous ethylene application and pathogen infection to PR gene induction. In this study EREBP3 was used as bait in a yeast two-hybrid interaction trap with a tobacco cDNA library as prey to isolate signal transduction pathway intermediates that interact with EREBPs. One of the strongest interactors was found to encode a nitrilase-like protein (NLP). Nitrilase is an enzyme involved in auxin biosynthesis. NLP interacted with other EREBP family members, namely tobacco EREBP2 and tomato (Lycopersicon esculentum L.) Pti4/5/6. The EREBP2-EREBP3 interaction with NLP required part of the DNA-binding domain. The specificity of interaction was further confirmed by protein-binding studies in solution. We propose that the EREBP-NLP interaction serves to regulate PR gene expression by sequestration of EREBPs in the cytoplasm.

1   This work was supported by the U.S. Department of Agriculture National Research Initiative Competitive Grants Program (no. 94-37100-0754) and by a Rockefeller Foundation Fellowship to P.X. This is journal paper no. 15,620 of the Purdue University Agricultural Experiment Station.
2   These authors contributed equally to this work.
3   Present address: Department of Plant Pathology, 4024 Throckmorton Plant Sciences Center, Kansas State University, Manhattan, KS 66506-5502.
*   Corresponding author; e-mail bressan{at}hort.purdue.edu; fax 1-765-494-0391.

Plant Physiol. (1998) 118: 867-874
Copyright Clearance Center:   0032-0889/98/118//08
© 1998 American Society of Plant Physiologists




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