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(Received for publication, January 29, 1997, and in revised form, March 4, 1997)
From the Neurobiotechnology Center, Ohio State University,
Columbus, Ohio 43210
Hydroxy fatty acids from plant cutin were shown
previously to induce the expression of the cutinase gene via a
palindromic sequence located at
Volume 272, Number 19,
Issue of May 9, 1997
pp. 12462-12467
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
159 base pairs of the cutinase gene
in Fusarium solani f. sp. pisi (Nectria
hematococca mating type VI). Of the two overlapping palindromes
in this sequence, palindrome 2 was found to be essential for the
inducibility of cutinase by hydroxy fatty acids. Screening of a phage
expression library with the concatenated palindrome 2 as probe detected
a distinct cDNA clone encoding a polypeptide designated cutinase
transcription factor 1
(CTF1) with a calculated molecular weight
of 101,109. This protein contains a Cys6Zn2
binuclear cluster motif sharing homology to the
Cys6Zn2 binuclear cluster DNA-binding domains
of transcription factors from Saccharomyces cerevisiae,
S. carlsbergensis, Kluyveromyces lactis,
Neurospora crassa, Aspergillus nidulans, and A. flavus. CTF1, expressed in Escherichia coli,
showed specific binding to the palindrome 2 DNA fragment but not to
palindrome 1 or mutant palindrome 2 DNA fragments, suggesting specific
binding of CTF1 to palindrome 2. When CTF1 was expressed as a
fusion protein with the nuclear localization sequence of SV40 in yeast,
it transactivated the native cutinase promoter fused to the
chloramphenicol acetyl transferase (cat) gene. Mutation of
palindrome 2 but not palindrome 1 abolished this transactivation. Thus,
CTF1 positively acts in vivo by binding selectively to
palindrome 2 of the cutinase gene promoter.
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