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Volume 271, Number 41,
Issue of October 11, 1996
pp. 25624-25629
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
Different Inducibility of Expression of the Two Xylanase
Genes xyn1 and xyn2 in Trichoderma
reesei
(Received for publication, February 26, 1996, and in revised form, July 15, 1996)
Susanne
Zeilinger
,
Robert L.
Mach
,
Martin
Schindler
,
Petra
Herzog
and
Christian P.
Kubicek
From the Abteilung für Mikrobielle Biochemie, Institut
für Biochemische Technologie und Mikrobiologie, TU Wien,
A-1060 Wien, Austria
Regulation of formation of the extracellular
xylanase system of Trichoderma reesei QM 9414 during growth
on xylan, cellulose, and replacement onto a number of soluble inducers
was investigated by Northern analysis of xyn1 and
xyn2 transcripts and by the use of the Escherichia
coli hph (hygromycin B-phosphotransferase-encoding) gene as a
reporter. Whereas the xyn1 promoter is active in the
presence of xylan and xylose, and virtually silenced in the presence of
glucose, the xyn2 promoter enables basal transcription at a
low level, but is enhanced in the presence of xylan and xylobiose and
also of sophorose or cellobiose. The respective regulatory nucleotide
regions were localized on a 221-base pair fragment and a 55-base pair
fragment of the xyn1 and xyn2 5 -upstream
noncoding sequences, respectively. Electrophoretic mobility shift
assays, using cell-free extracts, identified induction-specific
protein-DNA complexes: one complex of high mobility was observed under
basal, noninduced conditions (glucose) with xyn2, which was
in part replaced by a slow-migrating complex upon induction by xylan or
sophorose. Both complexes bound to a CCAAT box. With xyn1,
the induced complex also binds to a CCAAT box, but this binding is not
observed in the presence of the carbon catabolite repressor Cre1, which
binds to a nearby located consensus motif.

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Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.
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