A xylanase produced by the rumen anaerobic protozoan Polyplastron multivesiculatum shows close sequence similarity to family 11 xylanases from gram-positive bacteria

E Devillard, C J Newbold, K P Scott, E Forano, R J Wallace, J P Jouany, H J Flint

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

We report for the first time the cloning and characterisation of a protozoal enzyme involved in plant cell wall polysaccharide degradation. A cDNA library was constructed from the ruminal protozoan Polyplastron multivesiculatum and a stable clone expressing xylanase activity was isolated. The encoded enzyme belongs to the glycoside hydrolase family 11, and phylogenetic analysis indicates a closer relationship with catalytic domains from Gram-positive bacteria than the other fibrolytic eukaryotes from the rumen, the anaerobic fungi.

Original languageEnglish
Pages (from-to)145-52
Number of pages8
JournalFEMS Microbiology Letters
Volume181
Issue number1
DOIs
Publication statusPrint publication - 1 Dec 1999
Externally publishedYes

Fingerprint

Rumen
Gram-Positive Bacteria
Glycoside Hydrolases
Plant Cells
Enzymes
Eukaryota
Gene Library
Cell Wall
Polysaccharides
Organism Cloning
Catalytic Domain
Fungi
Clone Cells

Keywords

  • Amino Acid Sequence
  • Anaerobiosis
  • Animals
  • Base Sequence
  • Ciliophora/enzymology
  • DNA, Complementary/genetics
  • Electrophoresis, Polyacrylamide Gel
  • Glucans/metabolism
  • Gram-Positive Bacteria/enzymology
  • Immunoblotting
  • Molecular Sequence Data
  • Phylogeny
  • Rumen/parasitology
  • Sequence Analysis, DNA
  • Xylan Endo-1,3-beta-Xylosidase
  • Xylans/metabolism
  • Xylosidases/chemistry

Cite this

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title = "A xylanase produced by the rumen anaerobic protozoan Polyplastron multivesiculatum shows close sequence similarity to family 11 xylanases from gram-positive bacteria",
abstract = "We report for the first time the cloning and characterisation of a protozoal enzyme involved in plant cell wall polysaccharide degradation. A cDNA library was constructed from the ruminal protozoan Polyplastron multivesiculatum and a stable clone expressing xylanase activity was isolated. The encoded enzyme belongs to the glycoside hydrolase family 11, and phylogenetic analysis indicates a closer relationship with catalytic domains from Gram-positive bacteria than the other fibrolytic eukaryotes from the rumen, the anaerobic fungi.",
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author = "E Devillard and Newbold, {C J} and Scott, {K P} and E Forano and Wallace, {R J} and Jouany, {J P} and Flint, {H J}",
year = "1999",
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language = "English",
volume = "181",
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A xylanase produced by the rumen anaerobic protozoan Polyplastron multivesiculatum shows close sequence similarity to family 11 xylanases from gram-positive bacteria. / Devillard, E; Newbold, C J; Scott, K P; Forano, E; Wallace, R J; Jouany, J P; Flint, H J.

In: FEMS Microbiology Letters, Vol. 181, No. 1, 01.12.1999, p. 145-52.

Research output: Contribution to journalArticle

TY - JOUR

T1 - A xylanase produced by the rumen anaerobic protozoan Polyplastron multivesiculatum shows close sequence similarity to family 11 xylanases from gram-positive bacteria

AU - Devillard, E

AU - Newbold, C J

AU - Scott, K P

AU - Forano, E

AU - Wallace, R J

AU - Jouany, J P

AU - Flint, H J

PY - 1999/12/1

Y1 - 1999/12/1

N2 - We report for the first time the cloning and characterisation of a protozoal enzyme involved in plant cell wall polysaccharide degradation. A cDNA library was constructed from the ruminal protozoan Polyplastron multivesiculatum and a stable clone expressing xylanase activity was isolated. The encoded enzyme belongs to the glycoside hydrolase family 11, and phylogenetic analysis indicates a closer relationship with catalytic domains from Gram-positive bacteria than the other fibrolytic eukaryotes from the rumen, the anaerobic fungi.

AB - We report for the first time the cloning and characterisation of a protozoal enzyme involved in plant cell wall polysaccharide degradation. A cDNA library was constructed from the ruminal protozoan Polyplastron multivesiculatum and a stable clone expressing xylanase activity was isolated. The encoded enzyme belongs to the glycoside hydrolase family 11, and phylogenetic analysis indicates a closer relationship with catalytic domains from Gram-positive bacteria than the other fibrolytic eukaryotes from the rumen, the anaerobic fungi.

KW - Amino Acid Sequence

KW - Anaerobiosis

KW - Animals

KW - Base Sequence

KW - Ciliophora/enzymology

KW - DNA, Complementary/genetics

KW - Electrophoresis, Polyacrylamide Gel

KW - Glucans/metabolism

KW - Gram-Positive Bacteria/enzymology

KW - Immunoblotting

KW - Molecular Sequence Data

KW - Phylogeny

KW - Rumen/parasitology

KW - Sequence Analysis, DNA

KW - Xylan Endo-1,3-beta-Xylosidase

KW - Xylans/metabolism

KW - Xylosidases/chemistry

U2 - 10.1111/j.1574-6968.1999.tb08837.x

DO - 10.1111/j.1574-6968.1999.tb08837.x

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JO - FEMS Microbiology Letters

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