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Plant Physiol, February 2001, Vol. 125, pp. 595-603
Involvement of a Nuclear-Encoded Basic Helix-Loop-Helix Protein
in Transcription of the Light-Responsive Promoter of
psbD1
Kyoko
Baba,2*
Takeshi
Nakano,
Kazutoshi
Yamagishi, and
Shigeo
Yoshida
RIKEN, The Institute of Physical and Chemical Research,
Wako, Saitama 351-0198, Japan
In the chloroplast psbD light-responsive promoter
(LRP), a highly conserved sequence exists upstream from the bacterial
 10/35 elements. Multiple sequence-specific DNA binding proteins are predicted to bind to the conserved sequence as transcription factors. Using yeast one-hybrid screening of an Arabidopsis cDNA library, a
possible DNA binding protein of the psbD LRP upstream
sequence was identified. The protein, designated PTF1, is a novel
protein of 355 amino acids (estimated molecular weight of 39.6)
that contains a basic helix-loop-helix DNA binding motif in the
predicted N-terminal region of the mature protein. Transient expression
assay of PTF1-GFP fusion protein showed that PTF1 was localized in
chloroplasts. Using the modified DNA sequence in the one-hybrid system,
the ACC repeat was shown to be essential for PTF1 binding. The
rate of psbD LRP mRNA accumulation was reduced in a
T-DNA-inserted Arabidopsis ptf1 mutant. Compared with wild-type plants,
the mutant had pale green cotyledons and its growth was inhibited under
short-day conditions. These results suggest that PTF1 is a trans-acting factor of the psbD LRP.
1
This research was supported by a Grant-in-Aid
from the Ministry of Science, Education and Culture of Japan (no.
11151230 to T.N. and K.B.). K.B. and K.Y. were supported by the Special
Postdoctoral Researchers' Program of RIKEN.
2
Present address: Department of Forest Genetics and Plant
Physiology, The Swedish University of Agricultural Sciences, S-901 83 Umeå, Sweden.
*
Corresponding author; e-mail kyoko.baba{at}genfys.slu.se; fax
46-90-786-5901.
© 2001 American Society of Plant Physiologists
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