First published online February 24, 2002; 10.1104/pp.010642
Plant Physiol, March 2002, Vol. 128, pp. 833-843
Interaction of the Arabidopsis E2F and DP Proteins Confers
Their Concomitant Nuclear Translocation and Transactivation
Shunichi
Kosugi and
Yuko
Ohashi*
Molecular Genetics Department, National Institute of Agrobiological
Sciences, Tsukuba, Ibaraki 305-8602, Japan
E2F transcription factors are required for the progression
and arrest of the cell cycle in animals. Like animals, plants have evolved to conserve the E2F family. The Arabidopsis genome encodes E2F
and DP proteins that share a high similarity with the animal E2F and DP
families. Here, we show that Arabidopsis E2F and DP proteins are not
predominantly localized to the nucleus in analyses with green
fluorescent protein, and that the complete nuclear localization of some
members is driven by the co-expression of their specific partner
proteins. Both AtE2F1 and AtE2F3 were translocated to the nucleus and
transactivate an E2F reporter gene when co-expressed with DPa but not
DPb. In contrast, AtE2F2 was inactive for both nuclear translocation
and transactivation even when Dpa or DPb was co-expressed. Because the
DNA binding activities of the three E2Fs are equally stimulated by the
interaction with DPa or DPb in vitro, the observed transactivation of
AtE2F1 and AtE2F3 is DPa specific and nuclear import dependent. A green
fluorescent protein fusion with an AtE2F3 mutant, in which a conserved
nuclear export signal-like sequence in the dimerization domain was
deleted, was localized to the nucleus. Thus, the concomitant nuclear
translocation seems to be conferred by the DPa interaction to release
an activity that inhibits an intrinsic nuclear import activity of
AtE2Fs. Furthermore, the nuclear translocation of AtE2F3 stimulated by DPa was abolished by the deletion of the N-terminal region of AtE2F3,
which is conserved among all the E2F proteins identified in plants to
date. Replacement of the N-terminal region of AtE2F3 with a canonical
nuclear localization signal only partially mimicked the effect of the
DPa co-expression, demonstrating the function of plant E2F distinct
from that observed for animal E2Fs. These observations suggest that the
function of plant E2F and DP proteins is primarily controlled by their
nuclear localization mediated by the interaction with specific partner proteins.
*
Corresponding author; e-mail yohashi{at}nias.affrc.go.jp; fax
81-298-38-7469.
© 2002 American Society of Plant Physiologists
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