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Applied and Environmental Microbiology, June 1999, p. 2453-2460, Vol. 65, No. 6
Molecular Genetics of Industrial
Microorganisms, Wageningen Agricultural University, NL-6703 HA
Wageningen, The Netherlands
Received 4 January 1999/Accepted 1 April 1999
A gene encoding a third
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Differential Expression of Three
-Galactosidase
Genes and a Single
-Galactosidase Gene from Aspergillus
niger

-galactosidase (AglB) from
Aspergillus niger has been cloned and sequenced. The gene
consists of an open reading frame of 1,750 bp containing six introns.
The gene encodes a protein of 443 amino acids which contains a
eukaryotic signal sequence of 16 amino acids and seven putative
N-glycosylation sites. The mature protein has a calculated molecular
mass of 48,835 Da and a predicted pI of 4.6. An alignment of the AglB
amino acid sequence with those of other
-galactosidases revealed
that it belongs to a subfamily of
-galactosidases that also includes A. niger AglA. A. niger AglC belongs to a
different subfamily that consists mainly of prokaryotic
-galactosidases. The expression of aglA,
aglB, aglC, and lacA, the latter of
which encodes an A. niger
-galactosidase, has been
studied by using a number of monomeric, oligomeric, and polymeric
compounds as growth substrates. Expression of aglA is only
detected on galactose and galactose-containing oligomers and polymers.
The aglB gene is expressed on all of the carbon sources
tested, including glucose. Elevated expression was observed on xylan,
which could be assigned to regulation via XlnR, the xylanolytic
transcriptional activator. Expression of aglC was only
observed on glucose, fructose, and combinations of glucose with xylose
and galactose. High expression of lacA was detected on
arabinose, xylose, xylan, and pectin. Similar to aglB, the
expression on xylose and xylan can be assigned to regulation via XlnR.
All four genes have distinct expression patterns which seem to mirror
the natural substrates of the encoded proteins.
*
Corresponding author. Mailing address: Dreijenlaan 2, NL-6703 HA Wageningen, The Netherlands. Phone: 31 (0) 317 482865. Fax: 31 (0) 317 484011. E-mail:
office{at}algemeen.mgim.wau.nl.
Present address: Instituto de Agroquimica y Technologia de
Alimentos CSIC, 46100 Burjassot, Valencia, Spain.
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