Nucleic Acids Research, Vol 25, Issue 4 756-763, Copyright © 1997 by Oxford University Press
D Schmitz, S Lohmer, F Salamini and RD Thompson
The maize (Zea mays L.) endosperm specific transcription factor, encoded by
the Opaque-2(O2) locus, functions in vivo to activate transcription from
its target promoters.O2 regulates the expression of a major storage protein
class, the 22 kDa zeins, and of a type I ribosome inactivating protein,
b-32, during maturation phase endosperm development. The coding sequence of
O2, which indicates it to be a member of the basic region-leucine zipper
(bZIP) class of DNA-binding proteins, contains a number of regions rich in
either proline or acidic residues which are candidates for activation
domains. In functional assays using tobacco mesophyll protoplasts, the
level of transactivation conferred by a series of O2-deletion constructs
was tested using as a reporter a fusion of the b-32 target promoter to
beta- glucuronidase (GUS). The results indicate that O2 has a single acidic
activation domain, located near the N-terminus of the protein (amino acids
41-91). The ability of a shorter part of this domain (amino acids 39-82) to
confer transactivation was also demonstrated in domain swapping
experiments, using fusions of the O2 polypeptide sequence to the
DNA-binding domain of the parsley (Petroselinum crispum) transcription
factor CPRF1.
ARTICLES
The activation domain of the maize transcription factor Opaque-2 resides in a single acidic region
Max-Planck-Institut fur Zuchtungsforschung, Koln, Germany.
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