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

FEMS Microbiol Lett. 1999 Dec 1;181(1):145-52. doi: 10.1111/j.1574-6968.1999.tb08837.x.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

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

Substances

  • DNA, Complementary
  • Glucans
  • Xylans
  • Xylosidases
  • Xylan Endo-1,3-beta-Xylosidase

Associated data

  • GENBANK/AJ009828