Source:http://linkedlifedata.com/resource/pubmed/id/12471499
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2002-12-9
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pubmed:abstractText |
The regulation of formation of the single intracellular beta-galactosidase activity of Aspergillus nidulans was investigated. beta-Galactosidase was not formed during growth on glucose or glycerol, but was rapidly induced during growth on lactose or D-galactose. L-Arabinose, and -- with lower efficacy -- D-xylose also induced beta-galactosidase activity. Addition of glucose to cultures growing on lactose led to a rapid decrease in beta-galactosidase activity. In contrast, in cultures growing on D-galactose, addition of glucose decreased the activity of beta-galactosidase only slightly. Glucose inhibited the uptake of lactose, but not of D-galactose, and required the carbon catabolite repressor CreA for this. In addition, CreA also repressed the formation of basal levels of beta-galactosidase and partially interfered with the induction of beta-galactosidase by D-galactose, L-arabinose, and D-xylose. D-Galactose phosphorylation was not necessary for beta-galactosidase induction, since induction by D-galactose occurred in an A. nidulans mutant defective in galactose kinase, and by the non-metabolizable D-galactose analogue fucose in the wild-type strain. Interestingly, a mutant in galactose-1-phosphate uridylyl transferase produced beta-galactosidase at a low, constitutive level even on glucose and glycerol and was no longer inducible by D-galactose, whereas it was still inducible by L-arabinose. We conclude that biosynthesis of the intracellular beta-galactosidase of A. nidulans is regulated by CreA, partially repressed by galactose-1-phosphate uridylyl transferase, and induced by D-galactose and L-arabinose in independent ways.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Galactose,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Glycerol,
http://linkedlifedata.com/resource/pubmed/chemical/Lactose,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase,
http://linkedlifedata.com/resource/pubmed/chemical/hemicellulose
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0302-8933
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
179
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7-14
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12471499-Aspergillus nidulans,
pubmed-meshheading:12471499-Galactose,
pubmed-meshheading:12471499-Glucose,
pubmed-meshheading:12471499-Glycerol,
pubmed-meshheading:12471499-Kluyveromyces,
pubmed-meshheading:12471499-Lactose,
pubmed-meshheading:12471499-Mutation,
pubmed-meshheading:12471499-Polysaccharides,
pubmed-meshheading:12471499-beta-Galactosidase
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pubmed:year |
2002
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pubmed:articleTitle |
Regulation of formation of the intracellular beta-galactosidase activity of Aspergillus nidulans.
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pubmed:affiliation |
Department of Microbiology and Biotechnology, Faculty of Science, University of Debrecen, 4010, P.O.Box 63, Debrecen, Hungary.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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