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Plant Cell, Vol. 12, 1477-1490, August 2000, Copyright © 2000, American Society of Plant Physiologists

PBF-2 Is a Novel Single-Stranded DNA Binding Factor Implicated in PR-10a Gene Activation in Potato

Darrell Desveauxa, Charles Desprésa, Alexandre Joyeuxa, Rajagopal Subramaniama, and Normand Brissona
a Department of Biochemistry, Université de Montréal, Montréal, Québec, Canada H3C 3J7

Correspondence to: Normand Brisson, at Department of Biochemistry, Université de Montréal, 2900 Blvd. Edouard-Montpetit, Montréal, Québec, Canada H3T 1J4., normand.brisson{at}umontreal.ca (E-mail)

Elicitor-induced activation of the potato pathogenesis-related gene PR-10a requires a 30-bp promoter sequence termed the ERE (elicitor response element) that is bound by the nuclear factor PBF-2 (PR-10a binding factor 2). In this study, PBF-2 has been purified to near homogeneity from elicited tubers through a combination of anion-exchange and DNA affinity chromatography. Evidence demonstrates that inactive PBF-2 is stored in the nuclei of fresh tubers and becomes available for binding to the ERE upon elicitation. A protein with an apparent molecular mass of 24 kD (p24) is a DNA binding component of PBF-2. A cDNA encoding p24 has been cloned and encodes a novel protein with a potential transcriptional activation domain that could also act as a single-stranded DNA binding domain. Both PBF-2 and the cDNA-encoded protein bind with high affinity to the single-stranded form of the ERE in a sequence-specific manner. The inverted repeat sequence of the ERE, TGACAnnnnTGTCA, is critical for binding of this factor in vitro and for PR-10a expression in vivo, supporting the role of PBF-2 as a transcriptional regulator.




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