[Cloning of an endo-1,4-beta-xylanase gene from Penicillium canescens and construction of multicopy strains].
The complete gene xylA that encodes endo-1,4-beta-xylanase secreted by Penicillium canescens was cloned and sequenced. The coding region of the gene is separated by eight introns. The protein comprises 302 amino acids of the mature protein and 25 amino acids of the signal peptide. The xylanase of P. canescens belongs to the glycosyl hydrolase family 10. Nucleotide sequences for binding catabolite repression protein CREA and transactivator protein were detected in the promoter region. A set of multicopy strains displaying a seven-eightfold increase in xylanase yield was obtained. The fraction of xylanase in most productive strains amounted to 30-50% of the total secreted protein.
Serebrianyĭ
V A
VA
State Research Center of Genetics and Selection of Industrial Microorganisms (GosNIIGenetika), Moscow, 113545 Russia.
Vavilova
E A
EA
Chulkin
A M
AM
Vinetskiĭ
Iu P
IuP
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004271:DNA, Fungal; D004591:Electrophoresis, Polyacrylamide Gel; D043364:Endo-1,4-beta Xylanases; D005800:Genes, Fungal; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D010407:Penicillium / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid; D013696:Temperature; D015534:Trans-Activators / Q000378:metabolism; D014995:Xylosidases / Q000235:genetics* / Q000378:metabolism
D004271:DNA, Fungal; D015534:Trans-Activators; D014995:Xylosidases; D043364:Endo-1,4-beta Xylanases