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

Estelle Devillard; C. J. Newbold; Karen P. Scott; Evelyne Forano; R. John Wallace; Jean-Pierre Jouany; Harry J. Flint

doi:10.1016/S0378-1097(99)00525-X

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

Estelle Devillard, C. J. Newbold, Karen P. Scott, Evelyne Forano, R. John Wallace, Jean-Pierre Jouany, Harry J. Flint

Department of Life Sciences

Research output: Contribution to journal › Article › peer-review

54 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 language	English
Pages (from-to)	145-152
Number of pages	8
Journal	FEMS Microbiology Letters
Volume	181
Issue number	1
Early online date	15 Nov 1999
DOIs	https://doi.org/10.1016/S0378-1097(99)00525-X
Publication status	Published - 01 Dec 1999

Keywords

POPULATIONS
PROTEIN
rumen
CELLULOLYTIC BACTERIA
protozoa
CELLULASES
GENE
FUNGI
DIGESTION
ENZYMES
Polyplastron multivesiculatum
DOMAINS
SHEEP
xylanase
Protozoa
Rumen
Xylanase

Access to Document

10.1016/S0378-1097(99)00525-X

Permanent link

Persistent link

Cite this

@article{fe0de01561154c86b14424d9b3040a9d,

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.",

keywords = "POPULATIONS, PROTEIN, rumen, CELLULOLYTIC BACTERIA, protozoa, CELLULASES, GENE, FUNGI, DIGESTION, ENZYMES, Polyplastron multivesiculatum, DOMAINS, SHEEP, xylanase, Protozoa, Rumen, Xylanase",

author = "Estelle Devillard and Newbold, {C. J.} and Scott, {Karen P.} and Evelyne Forano and Wallace, {R. John} and Jean-Pierre Jouany and Flint, {Harry J.}",

note = "Funding Information: We are grateful for joint support from INRA (France) and from the Scottish Office Agriculture, Fisheries and Environment Department (SOAFED, UK) for this project. E.D. is supported by a grant {\textquoteleft}Cotutelle de th{\`e}se{\textquoteright} from the French MENRT. We thank L. Millet for the gift of fungal DNA.",

year = "1999",

month = dec,

day = "1",

doi = "10.1016/S0378-1097(99)00525-X",

language = "English",

volume = "181",

pages = "145--152",

journal = "FEMS Microbiology Letters",

issn = "0378-1097",

publisher = "Oxford University Press",

number = "1",

}

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, Estelle

AU - Newbold, C. J.

AU - Scott, Karen P.

AU - Forano, Evelyne

AU - Wallace, R. John

AU - Jouany, Jean-Pierre

AU - Flint, Harry J.

N1 - Funding Information: We are grateful for joint support from INRA (France) and from the Scottish Office Agriculture, Fisheries and Environment Department (SOAFED, UK) for this project. E.D. is supported by a grant ‘Cotutelle de thèse’ from the French MENRT. We thank L. Millet for the gift of fungal DNA.

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 - POPULATIONS

KW - PROTEIN

KW - rumen

KW - CELLULOLYTIC BACTERIA

KW - protozoa

KW - CELLULASES

KW - GENE

KW - FUNGI

KW - DIGESTION

KW - ENZYMES

KW - Polyplastron multivesiculatum

KW - DOMAINS

KW - SHEEP

KW - xylanase

KW - Protozoa

KW - Rumen

KW - Xylanase

UR - http://www.scopus.com/inward/record.url?scp=0032723601&partnerID=8YFLogxK

U2 - 10.1016/S0378-1097(99)00525-X

DO - 10.1016/S0378-1097(99)00525-X

M3 - Article

SN - 0378-1097

VL - 181

SP - 145

EP - 152

JO - FEMS Microbiology Letters

JF - FEMS Microbiology Letters

IS - 1

ER -

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

Abstract

Keywords

Access to Document

Permanent link

Other files and links

Fingerprint

Cite this