Penicillium purpurogenum produces a family 1 acetyl xylan esterase containing a carbohydrate-binding module: characterization of the protein and its gene

Felipe Gordillo, Valentina Caputo, Alessandra Peirano, Renato Chavez, Jozef Van Beeumen, Isabel Vandenberghe, Marc Claeyssens, Paulina Bull, María Cristina Ravanal, Jaime Eyzaguirre

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

At least three acetyl xylan esterases (AXE I, II and III) are secreted by Penicillium purpurogenum. This publication describes more detailed work on AXE I and its gene. AXE I binds cellulose but not xylan; it is glycosylated and inactivated by phenylmethylsulphonyl fluoride, showing that it is a serine esterase. The axe1 gene presents an open reading frame of 1278 bp, including two introns of 68 and 61 bp; it codes for a signal peptide of 31 residues and a mature protein of 351 amino acids (molecular weight 36,693). AXE I has a modular structure: a catalytic module at the amino terminus belonging to family 1 of the carbohydrate esterases, a linker rich in serines and threonines, and a family 1 carboxy terminal carbohydrate binding module (CBM). The CBM is similar to that of AXE from Trichoderma reesei, (with a family 5 catalytic module) indicating that the genes for catalytic modules and CBMs have evolved separately, and that they have been linked by gene fusion. The promoter sequence of axe1 contains several putative sequences for binding of gene expression regulators also found in other family 1 esterase gene promoters. It is proposed that AXE I and II act in succession in xylan degradation; first, xylan is attacked by AXE I and other xylanases possessing CBMs (which facilitate binding to lignocellulose), followed by other enzymes acting mainly on soluble substrates.

Original languageEnglish
Pages (from-to)1129-1139
Number of pages11
JournalMycological Research
Volume110
Issue number10
DOIs
Publication statusPublished - 1 Oct 2006

Fingerprint

acetylxylan esterase
Talaromyces purpurogenus
Xylans
carbohydrate binding
Penicillium
xylan
esterases
carbohydrate
Carbohydrates
protein
gene
serine
Genes
Proteins
Trichoderma
genes
proteins
Gene Regulatory Networks
Gene Fusion
promoter regions

Keywords

  • AXE genes
  • Enzymes
  • Gene regulation
  • Xylan biodegradation

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Plant Science

Cite this

Gordillo, Felipe ; Caputo, Valentina ; Peirano, Alessandra ; Chavez, Renato ; Van Beeumen, Jozef ; Vandenberghe, Isabel ; Claeyssens, Marc ; Bull, Paulina ; Ravanal, María Cristina ; Eyzaguirre, Jaime. / Penicillium purpurogenum produces a family 1 acetyl xylan esterase containing a carbohydrate-binding module : characterization of the protein and its gene. In: Mycological Research. 2006 ; Vol. 110, No. 10. pp. 1129-1139.
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Gordillo, F, Caputo, V, Peirano, A, Chavez, R, Van Beeumen, J, Vandenberghe, I, Claeyssens, M, Bull, P, Ravanal, MC & Eyzaguirre, J 2006, 'Penicillium purpurogenum produces a family 1 acetyl xylan esterase containing a carbohydrate-binding module: characterization of the protein and its gene', Mycological Research, vol. 110, no. 10, pp. 1129-1139. https://doi.org/10.1016/j.mycres.2006.07.003

Penicillium purpurogenum produces a family 1 acetyl xylan esterase containing a carbohydrate-binding module : characterization of the protein and its gene. / Gordillo, Felipe; Caputo, Valentina; Peirano, Alessandra; Chavez, Renato; Van Beeumen, Jozef; Vandenberghe, Isabel; Claeyssens, Marc; Bull, Paulina; Ravanal, María Cristina; Eyzaguirre, Jaime.

In: Mycological Research, Vol. 110, No. 10, 01.10.2006, p. 1129-1139.

Research output: Contribution to journalArticle

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T2 - characterization of the protein and its gene

AU - Gordillo, Felipe

AU - Caputo, Valentina

AU - Peirano, Alessandra

AU - Chavez, Renato

AU - Van Beeumen, Jozef

AU - Vandenberghe, Isabel

AU - Claeyssens, Marc

AU - Bull, Paulina

AU - Ravanal, María Cristina

AU - Eyzaguirre, Jaime

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N2 - At least three acetyl xylan esterases (AXE I, II and III) are secreted by Penicillium purpurogenum. This publication describes more detailed work on AXE I and its gene. AXE I binds cellulose but not xylan; it is glycosylated and inactivated by phenylmethylsulphonyl fluoride, showing that it is a serine esterase. The axe1 gene presents an open reading frame of 1278 bp, including two introns of 68 and 61 bp; it codes for a signal peptide of 31 residues and a mature protein of 351 amino acids (molecular weight 36,693). AXE I has a modular structure: a catalytic module at the amino terminus belonging to family 1 of the carbohydrate esterases, a linker rich in serines and threonines, and a family 1 carboxy terminal carbohydrate binding module (CBM). The CBM is similar to that of AXE from Trichoderma reesei, (with a family 5 catalytic module) indicating that the genes for catalytic modules and CBMs have evolved separately, and that they have been linked by gene fusion. The promoter sequence of axe1 contains several putative sequences for binding of gene expression regulators also found in other family 1 esterase gene promoters. It is proposed that AXE I and II act in succession in xylan degradation; first, xylan is attacked by AXE I and other xylanases possessing CBMs (which facilitate binding to lignocellulose), followed by other enzymes acting mainly on soluble substrates.

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