Regulation of invertase in Aspergillus nidulans: effect of different carbon sources

Department of Botany, Microbial Biochemistry and Genetics Group, University of Nottingham, Nottingham NG7 2RD, UK ABSTRACT SUMMARY: Aspergillus nidulans produces an extracellular β-D-fructofuranoside fructohydrolase (invertase) when grown on a medium containing the β-fructofuranosides sucrose or raf...

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Published inJournal of general microbiology Vol. 137; no. 2; pp. 315 - 321
Main Authors Vainstein, M.H, Peberdy, J.F
Format Journal Article
LanguageEnglish
Published London Soc General Microbiol 01.02.1991
New York, NY Cambridge University Press
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ISSN0022-1287
1350-0872
1465-2080
DOI10.1099/00221287-137-2-315

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Abstract Department of Botany, Microbial Biochemistry and Genetics Group, University of Nottingham, Nottingham NG7 2RD, UK ABSTRACT SUMMARY: Aspergillus nidulans produces an extracellular β-D-fructofuranoside fructohydrolase (invertase) when grown on a medium containing the β-fructofuranosides sucrose or raffinose, indicating that synthesis is subject to induction by the substrate. On a growth medium containing sucrose, production was maximal at 15 h in cultures incubated at 28 C°. After this time the level of detectable invertase in the cultures declined. A proportion of the enzyme was secreted during the linear growth phase of the fungus. Various sugars were investigated for induction of invertase, but only the two β-fructofuranosides induced high production levels; with the other sugars, the enzyme was produced only at a low constitutive level. Mycelium grown under repressive conditions (1% glucose), rapidly produced invertase when transferred to sucrose-containing medium. After 80 min the invertase level in these cultures was 26-fold higher than the constitutive level. The repressive effect of other sugars, e.g. glucose and xylose, on invertase production was also demonstrated in this experimental system. Present address: Laboratorio de Microbiologia, Departamento de Biologia Celular, Universidade de Brasilia, Brasilia, DF, Brazil.
AbstractList Aspergillus nidulans produces an extracellular beta-D-fructofuranoside fructohydrolase (invertase) when grown on a medium containing the beta-fructofuranosides sucrose or raffinose, indicating that synthesis is subject to induction by the substrate. On a growth medium containing sucrose, production was maximal at 15 h in cultures incubated at 28 C degrees. After this time the level of detectable invertase in the cultures declined. A proportion of the enzyme was secreted during the linear growth phase of the fungus. Various sugars were investigated for induction of invertase, but only the two beta-fructofuranosides induced high production levels; with the other sugars, the enzyme was produced only at a low constitutive level. Mycelium grown under repressive conditions (1% glucose), rapidly produced invertase when transferred to sucrose-containing medium. After 80 min the invertase level in these cultures was 26-fold higher than the constitutive level. The repressive effect of other sugars, e.g. glucose and xylose, on invertase production was also demonstrated in this experimental system.
Department of Botany, Microbial Biochemistry and Genetics Group, University of Nottingham, Nottingham NG7 2RD, UK ABSTRACT SUMMARY: Aspergillus nidulans produces an extracellular β-D-fructofuranoside fructohydrolase (invertase) when grown on a medium containing the β-fructofuranosides sucrose or raffinose, indicating that synthesis is subject to induction by the substrate. On a growth medium containing sucrose, production was maximal at 15 h in cultures incubated at 28 C°. After this time the level of detectable invertase in the cultures declined. A proportion of the enzyme was secreted during the linear growth phase of the fungus. Various sugars were investigated for induction of invertase, but only the two β-fructofuranosides induced high production levels; with the other sugars, the enzyme was produced only at a low constitutive level. Mycelium grown under repressive conditions (1% glucose), rapidly produced invertase when transferred to sucrose-containing medium. After 80 min the invertase level in these cultures was 26-fold higher than the constitutive level. The repressive effect of other sugars, e.g. glucose and xylose, on invertase production was also demonstrated in this experimental system. Present address: Laboratorio de Microbiologia, Departamento de Biologia Celular, Universidade de Brasilia, Brasilia, DF, Brazil.
Aspergillus nidulans produces an extracellular beta -D-fructofuranoside fructohydrolase (invertase) when grown on a medium containing the beta -fructofuranosides sucrose or raffinose, indicating that synthesis is subject to induction by the substrate. On a growth medium containing sucrose, production was maximal at 15 h in cultures incubated at 28 C degree . After this time the level of detectable invertase in the cultures declined. A proportion of the enzyme was secreted during the linear growth phase of the fungus. Various sugars were investigated for induction of invertase, but only the two beta -fructofuranosides induced high production levels; with the other sugars, the enzyme was produced only at a low constitutive level. Mycelium grown under repressive conditions (1% glucose), rapidly produced invertase when transferred to sucrose-containing medium.
Aspergillus nidulans produces an extracellular β - d -fructofuranoside fructohydrolase (invertase) when grown on a medium containing the β -fructofuranosides sucrose or raffinose, indicating that synthesis is subject to induction by the substrate. On a growth medium containing sucrose, production was maximal at 15 h in cultures incubated at 28 C°. After this time the level of detectable invertase in the cultures declined. A proportion of the enzyme was secreted during the linear growth phase of the fungus. Various sugars were investigated for induction of invertase, but only the two β -fructofuranosides induced high production levels; with the other sugars, the enzyme was produced only at a low constitutive level. Mycelium grown under repressive conditions (1% glucose), rapidly produced invertase when transferred to sucrose-containing medium. After 80 min the invertase level in these cultures was 26-fold higher than the constitutive level. The repressive effect of other sugars, e.g. glucose and xylose, on invertase production was also demonstrated in this experimental system.
Aspergillus nidulans produces an extracellular beta-D-fructofuranoside fructohydrolase (invertase) when grown on a medium containing the beta-fructofuranosides sucrose or raffinose, indicating that synthesis is subject to induction by the substrate. On a growth medium containing sucrose, production was maximal at 15 h in cultures incubated at 28 C degrees. After this time the level of detectable invertase in the cultures declined. A proportion of the enzyme was secreted during the linear growth phase of the fungus. Various sugars were investigated for induction of invertase, but only the two beta-fructofuranosides induced high production levels; with the other sugars, the enzyme was produced only at a low constitutive level. Mycelium grown under repressive conditions (1% glucose), rapidly produced invertase when transferred to sucrose-containing medium. After 80 min the invertase level in these cultures was 26-fold higher than the constitutive level. The repressive effect of other sugars, e.g. glucose and xylose, on invertase production was also demonstrated in this experimental system.Aspergillus nidulans produces an extracellular beta-D-fructofuranoside fructohydrolase (invertase) when grown on a medium containing the beta-fructofuranosides sucrose or raffinose, indicating that synthesis is subject to induction by the substrate. On a growth medium containing sucrose, production was maximal at 15 h in cultures incubated at 28 C degrees. After this time the level of detectable invertase in the cultures declined. A proportion of the enzyme was secreted during the linear growth phase of the fungus. Various sugars were investigated for induction of invertase, but only the two beta-fructofuranosides induced high production levels; with the other sugars, the enzyme was produced only at a low constitutive level. Mycelium grown under repressive conditions (1% glucose), rapidly produced invertase when transferred to sucrose-containing medium. After 80 min the invertase level in these cultures was 26-fold higher than the constitutive level. The repressive effect of other sugars, e.g. glucose and xylose, on invertase production was also demonstrated in this experimental system.
Author Vainstein, M.H
Peberdy, J.F
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Cites_doi 10.3109/00365516009065404
10.1016/0092-8674(81)90071-4
10.1016/S0021-9258(18)61360-2
10.1128/MCB.1.5.469
10.1111/j.1432-1033.1975.tb04157.x
10.1128/JB.97.2.867-872.1969
10.1128/JB.92.4.1010-1015.1966
10.1177/12.6.448
10.1007/BF02046409
10.1139/m69-218
10.1016/S0021-9258(18)32963-6
10.1016/S0021-9258(18)93580-5
10.1016/0092-8674(82)90384-1
10.1016/0003-2697(69)90068-2
10.1111/j.1399-3054.1980.tb02678.x
10.1016/S0065-2660(08)60408-3
10.1007/BF00267327
10.1021/ac60147a030
10.1093/genetics/98.1.25
10.1021/bi00854a015
10.1007/BF00333160
10.1016/0003-9861(62)90322-3
10.1016/S0021-9258(18)93579-9
10.1016/S0022-2836(61)80072-7
10.1128/MCB.6.7.2324
10.1021/bi00778a020
10.1016/0092-8674(81)90064-7
10.1016/0003-2697(76)90527-3
10.1016/0031-9422(82)80120-9
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Issue 2
Keywords Sucrose
Enzyme
Induction
β-D-Fructofuranosidase
Biosynthesis
Repression
Raffinose
Fungi
Substrate
Regulation(control)
Aspergillus nidulans
Carbohydrate
Fungi Imperfecti
Kinetics
Thallophyta
Language English
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References Sarokin (R33) 1986; 6
Casanova (R6) 1987; 133
Hackel (R15) 1978; 164
Carlson (R4) 1982; 28
Esmon (R8) 1987; 262
Metzenberg (R20) 1962; 96
Gabriel (R9) 1969; 27
Olutiola (R26) 1980; 50
Jacob (R16) 1961; 3
Meachum (R19) 1971; 10
Trevithick (R34) 1966; 92
Galbraith (R10) 1969; 15
Eilers (R7) 1964; 12
Trimble (R35) 1983; 258
Gascon (R11) 1968; 243
Miller (R22) 1959; 31
Pontecorvo (R29) 1953; 5
Andres (R1) 1974; 10
Novick (R25) 1981; 25
Neumann (R24) 1967; 6
Metzenberg (R21) 1964; 89
Sargent (R32) 1969; 97
Carlson (R3) 1984
Perlman (R27) 1981; 25
Kratky (R17) 1975; 54
Lampen (R18) 1968; 34
Rodriguez (R31) 1981; 1
Vainstein (R36) 1990
Hackel (R14) 1975; 140
Neuberg (R23) 1950
Carlson (R5) 1981; 98
Gascon (R12) 1968; 243
Perlman (R28) 1982; 79
Gupta (R13) 1982; 21
Bradford (R2) 1976; 72
Raabo (R30) 1960; 12
References_xml – volume: 12
  start-page: 402
  year: 1960
  ident: R30
  article-title: On the enzymatic determination of blood glucose
  publication-title: Scandinavian Journal of Clinical Laboratory Investigation
  doi: 10.3109/00365516009065404
– volume: 25
  start-page: 525
  year: 1981
  ident: R27
  article-title: Distinct repressible mRNA for cytoplasmic and secreted yeast invertase are encoded by a single gene
  publication-title: Cell
  doi: 10.1016/0092-8674(81)90071-4
– volume: 262
  start-page: 4387
  year: 1987
  ident: R8
  article-title: Structure, assembly, and secretion of octameric invertase
  publication-title: Journal of Biological Chemistry
  doi: 10.1016/S0021-9258(18)61360-2
– volume: 1
  start-page: 469
  year: 1981
  ident: R31
  article-title: SUC1 gene of Saccharomyces: a structural gene for the large (glycoprotein) and small (carbohydrate-free) forms of invertase
  publication-title: Molecular and Cellular Biology
  doi: 10.1128/MCB.1.5.469
– volume: 54
  start-page: 459
  year: 1975
  ident: R17
  article-title: Mechanism of 2-deoxy-dglucose inhibition of cell-wall polysaccharide and glycoprotein biosynthesis in Saccharomyces cerevisiae
  publication-title: European Journal of Biochemistry
  doi: 10.1111/j.1432-1033.1975.tb04157.x
– volume: 97
  start-page: 867
  year: 1969
  ident: R32
  article-title: Gene-enzyme relationships in Neurospora invertase
  publication-title: Journal of Bacteriology
  doi: 10.1128/JB.97.2.867-872.1969
– start-page: 527
  volume-title: In The Enzymes
  year: 1950
  ident: R23
  article-title: Invertase
– volume: 92
  start-page: 1010
  year: 1966
  ident: R34
  article-title: Molecular sieving by Neurospora cell walls during secretion of invertase isoenzymes
  publication-title: Journal of Bacteriology
  doi: 10.1128/JB.92.4.1010-1015.1966
– volume: 12
  start-page: 448
  year: 1964
  ident: R7
  article-title: Localization of disaccharidases in extracts of Neurospora after electrophoresis in polyacrylamide gels
  publication-title: Journal of Histochemistry and Cytochemistry
  doi: 10.1177/12.6.448
– volume: 34
  start-page: 1
  year: 1968
  ident: R18
  article-title: External enzymes of yeast: their nature and formation
  publication-title: Antonie van Leeuwenhoek
  doi: 10.1007/BF02046409
– volume: 15
  start-page: 1207
  year: 1969
  ident: R10
  article-title: Changes in activity of certain enzymes of the tricarboxylic acid cycle and the glyoxylate cycle during the initiation of conidiation of Aspergillus niger
  publication-title: Canadian Journal of Microbiology
  doi: 10.1139/m69-218
– volume: 258
  start-page: 2562
  year: 1983
  ident: R35
  article-title: Glycoprotein biosynthesis in yeast
  publication-title: Journal of Biological Chemistry
  doi: 10.1016/S0021-9258(18)32963-6
– volume: 89
  start-page: 291
  year: 1964
  ident: R21
  article-title: Enzymically active subunits of Neurospora invertase
  publication-title: Biochimica et Biophysica Acta
– volume: 243
  start-page: 1573
  year: 1968
  ident: R12
  article-title: Comparative study of the properties of the purified internal and external invertases from yeast
  publication-title: Journal of Biological Chemistry
  doi: 10.1016/S0021-9258(18)93580-5
– volume: 133
  start-page: 2447
  year: 1987
  ident: R6
  article-title: Different molecular forms of invertase in the slime variant of Neurospora crassa: comparison with the wild-type strain
  publication-title: Journal of General Microbiology
– volume: 79
  start-page: 781
  year: 1982
  ident: R28
  article-title: Presecretory and cytoplasmic invertase polypeptides encoded by distinct mRNAs derived from the same structural gene differ by a signal sequence
– volume: 28
  start-page: 145
  year: 1982
  ident: R4
  article-title: Two differentially regulated mRNAs with different 5′ ends encode secreted and intracellular forms of yeast invertase
  publication-title: Cell
  doi: 10.1016/0092-8674(82)90384-1
– volume: 27
  start-page: 545
  year: 1969
  ident: R9
  article-title: Determination of enzymatic activity in polyacrylamide gels. I. Enzymes catalyzing the conversion of nonreducing substrates to reducing products
  publication-title: Analytical Biochemistry
  doi: 10.1016/0003-2697(69)90068-2
– volume: 50
  start-page: 26
  year: 1980
  ident: R26
  article-title: Extracellular invertase from Aspergillus flavus
  publication-title: Physiologia Plantarum
  doi: 10.1111/j.1399-3054.1980.tb02678.x
– volume: 5
  start-page: 141
  year: 1953
  ident: R29
  article-title: The genetics of Aspergillus nidulans
  publication-title: Advances in Genetics
  doi: 10.1016/S0065-2660(08)60408-3
– volume: 140
  start-page: 361
  year: 1975
  ident: R14
  article-title: Genetic control of invertase formation in Saccharomyces cerevisae I. Isolation and characterization of mutants affecting sucrose utilization
  publication-title: Molecular and General Genetics
  doi: 10.1007/BF00267327
– volume: 31
  start-page: 426
  year: 1959
  ident: R22
  article-title: Use of dinitrosalicylic acid reagent for determination of reducing sugars
  publication-title: Analytical Chemistry
  doi: 10.1021/ac60147a030
– volume: 98
  start-page: 25
  year: 1981
  ident: R5
  article-title: Mutants of yeast defective in sucrose utilization
  publication-title: Genetics
  doi: 10.1093/genetics/98.1.25
– volume: 6
  start-page: 468
  year: 1967
  ident: R24
  article-title: Purification and properties of yeast invertase
  publication-title: Biochemistry
  doi: 10.1021/bi00854a015
– volume: 10
  start-page: 15
  year: 1974
  ident: R1
  article-title: The production of invertase in Aspergillus nidulans with reference to the effects of glucose and sucrose
  publication-title: Microbios
– volume: 164
  start-page: 295
  year: 1978
  ident: R15
  article-title: Genetic control of invertase formation in Saccharomyces cerevisiae II. Isolation and characterization of mutants conferring invertase hyperproduction in strain EK-6B carrying the SUC3 Gene
  publication-title: Molecular and General Genetics
  doi: 10.1007/BF00333160
– volume: 96
  start-page: 468
  year: 1962
  ident: R20
  article-title: A gene affecting the repression of invertase and trehalase in Neurospora
  publication-title: Archives of Biochemistry and Biophysics
  doi: 10.1016/0003-9861(62)90322-3
– volume: 243
  start-page: 1567
  year: 1968
  ident: R11
  article-title: Purification of internal invertase of yeast
  publication-title: Journal of Biological Chemistry
  doi: 10.1016/S0021-9258(18)93579-9
– volume: 3
  start-page: 318
  year: 1961
  ident: R16
  article-title: Genetic regulatory mechanisms in the synthesis of protein
  publication-title: Journal of Molecular Biology
  doi: 10.1016/S0022-2836(61)80072-7
– year: 1990
  ident: R36
  article-title: Regulation and characterisation of invertase in Aspergillus nidulans
  publication-title: PhD thesis
– start-page: 341
  year: 1984
  ident: R3
  article-title: A single SUC gene encodes both cytoplasmic and secreted invertase in Saccharomyces
  publication-title: Protein Transport and Secretion
– volume: 6
  start-page: 2324
  year: 1986
  ident: R33
  article-title: Short repeated elements in the upstream regulatory region of the SUC2 gene of Saccharomyces cerevisiae
  publication-title: Molecular and Cellular Biology
  doi: 10.1128/MCB.6.7.2324
– volume: 10
  start-page: 326
  year: 1971
  ident: R19
  article-title: Chemical and physical studies of Neurospora crassa invertase. Molecular weight, amino acid and carbohydrate composition and quaternary structure
  publication-title: Biochemistry
  doi: 10.1021/bi00778a020
– volume: 25
  start-page: 461
  year: 1981
  ident: R25
  article-title: Order of events in the yeast secretory pathway
  publication-title: Cell
  doi: 10.1016/0092-8674(81)90064-7
– volume: 72
  start-page: 248
  year: 1976
  ident: R2
  article-title: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  publication-title: Analytical Biochemistry
  doi: 10.1016/0003-2697(76)90527-3
– volume: 21
  start-page: 1249
  year: 1982
  ident: R13
  article-title: Glucofructosan biosynthesis in Fusarium oxysporum: regulation and substrate specificity of fructosyl transferase and invertase
  publication-title: Phytochemistry
  doi: 10.1016/0031-9422(82)80120-9
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Snippet Department of Botany, Microbial Biochemistry and Genetics Group, University of Nottingham, Nottingham NG7 2RD, UK ABSTRACT SUMMARY: Aspergillus nidulans...
Aspergillus nidulans produces an extracellular β - d -fructofuranoside fructohydrolase (invertase) when grown on a medium containing the β -fructofuranosides...
Aspergillus nidulans produces an extracellular beta-D-fructofuranoside fructohydrolase (invertase) when grown on a medium containing the beta-fructofuranosides...
Aspergillus nidulans produces an extracellular beta -D-fructofuranoside fructohydrolase (invertase) when grown on a medium containing the beta...
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StartPage 315
SubjectTerms Aspergillus nidulans - enzymology
Aspergillus nidulans - growth & development
Aspergillus nidulellus
beta-Fructofuranosidase
Biological and medical sciences
Biotechnology
Carbohydrates - pharmacology
Culture Media
enzyme activity
Enzyme Induction
Enzyme Repression
fructose
Fructose - pharmacology
Fundamental and applied biological sciences. Psychology
glucose
Glucose - pharmacology
Glycoside Hydrolases - biosynthesis
growth
Growth, nutrition, metabolism, transports, enzymes. Molecular biology
Microbiology
mycelium
Mycology
raffinose
secretion
substrates
sucrose
Sucrose - pharmacology
synthesis
xylose
Xylose - pharmacology
Title Regulation of invertase in Aspergillus nidulans: effect of different carbon sources
URI http://mic.sgmjournals.org/cgi/content/abstract/137/2/315
https://www.ncbi.nlm.nih.gov/pubmed/2016586
https://www.proquest.com/docview/15864460
https://www.proquest.com/docview/80514035
Volume 137
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