A BIFUNCTIONAL ENZYME, WITH SEPARATE XYLANASE AND BETA(1,3-1,4)-GLUCANASE DOMAINS, ENCODED BY THE XYND GENE OF RUMINOCOCCUS-FLAVEFACIENS

H J FLINT, J MARTIN, C A MCPHERSON, A S DANIEL, J X ZHANG

Research output: Contribution to journalArticle

108 Citations (Scopus)

Abstract

Adjacent regions of a Ruminococcus flavefaciens 17 DNA fragment were found to encode xylanase and beta(1,3-1,4)-glucanase activities. Sequencing of this fragment showed that both activities are encoded by a single 2,406-bp open reading frame corresponding to the xynD gene. The predicted product has a characteristic signal sequence that is followed by an amino-terminal domain related to family G xylanases, while the carboxy-terminal domain is related to beta(1,3-1,4)-glucanases from several other bacterial species. These two domains are connected by a region of unknown function that consists of 309 amino acids and includes a 30-amino-acid threonine-rich sequence. A polypeptide having a molecular weight of approximately 90,000 and exhibiting xylanase and beta(1,3-1,4)-glucanase activities was detected in Escherichia coli cells carrying the cloned xynD gene. This is one of the first cases in which a microbial polysaccharidase has been shown to carry separate catalytic domains active against different plant cell wall polysaccharides within the same polypeptide. xynD is one of a family of related genes in R. flavefaciens that encode enzymes having multiple catalytic domains, and the amino terminus of XYLD exhibits a high degree of similarity with the corresponding regions of another xylanase, XYLA, which carries two different xylanase catalytic domains.

Original languageEnglish
Pages (from-to)2943-2951
Number of pages9
JournalJournal of Bacteriology
Volume175
Issue number10
Publication statusPublished - May 1993

Keywords

  • NUCLEOTIDE-SEQUENCE
  • MOLECULAR-CLONING
  • BACILLUS-PUMILUS
  • BETA-GLUCANASE
  • DNA-SEQUENCE
  • EXPRESSION
  • RUMEN
  • BACTERIA
  • SUBTILIS

Cite this

A BIFUNCTIONAL ENZYME, WITH SEPARATE XYLANASE AND BETA(1,3-1,4)-GLUCANASE DOMAINS, ENCODED BY THE XYND GENE OF RUMINOCOCCUS-FLAVEFACIENS. / FLINT, H J ; MARTIN, J ; MCPHERSON, C A ; DANIEL, A S ; ZHANG, J X .

In: Journal of Bacteriology, Vol. 175, No. 10, 05.1993, p. 2943-2951.

Research output: Contribution to journalArticle

@article{cf81de6a46a2494fb427013b200757b6,
title = "A BIFUNCTIONAL ENZYME, WITH SEPARATE XYLANASE AND BETA(1,3-1,4)-GLUCANASE DOMAINS, ENCODED BY THE XYND GENE OF RUMINOCOCCUS-FLAVEFACIENS",
abstract = "Adjacent regions of a Ruminococcus flavefaciens 17 DNA fragment were found to encode xylanase and beta(1,3-1,4)-glucanase activities. Sequencing of this fragment showed that both activities are encoded by a single 2,406-bp open reading frame corresponding to the xynD gene. The predicted product has a characteristic signal sequence that is followed by an amino-terminal domain related to family G xylanases, while the carboxy-terminal domain is related to beta(1,3-1,4)-glucanases from several other bacterial species. These two domains are connected by a region of unknown function that consists of 309 amino acids and includes a 30-amino-acid threonine-rich sequence. A polypeptide having a molecular weight of approximately 90,000 and exhibiting xylanase and beta(1,3-1,4)-glucanase activities was detected in Escherichia coli cells carrying the cloned xynD gene. This is one of the first cases in which a microbial polysaccharidase has been shown to carry separate catalytic domains active against different plant cell wall polysaccharides within the same polypeptide. xynD is one of a family of related genes in R. flavefaciens that encode enzymes having multiple catalytic domains, and the amino terminus of XYLD exhibits a high degree of similarity with the corresponding regions of another xylanase, XYLA, which carries two different xylanase catalytic domains.",
keywords = "NUCLEOTIDE-SEQUENCE, MOLECULAR-CLONING, BACILLUS-PUMILUS, BETA-GLUCANASE, DNA-SEQUENCE, EXPRESSION, RUMEN, BACTERIA, SUBTILIS",
author = "FLINT, {H J} and J MARTIN and MCPHERSON, {C A} and DANIEL, {A S} and ZHANG, {J X}",
year = "1993",
month = "5",
language = "English",
volume = "175",
pages = "2943--2951",
journal = "Journal of Bacteriology",
issn = "0021-9193",
publisher = "American Society for Microbiology",
number = "10",

}

TY - JOUR

T1 - A BIFUNCTIONAL ENZYME, WITH SEPARATE XYLANASE AND BETA(1,3-1,4)-GLUCANASE DOMAINS, ENCODED BY THE XYND GENE OF RUMINOCOCCUS-FLAVEFACIENS

AU - FLINT, H J

AU - MARTIN, J

AU - MCPHERSON, C A

AU - DANIEL, A S

AU - ZHANG, J X

PY - 1993/5

Y1 - 1993/5

N2 - Adjacent regions of a Ruminococcus flavefaciens 17 DNA fragment were found to encode xylanase and beta(1,3-1,4)-glucanase activities. Sequencing of this fragment showed that both activities are encoded by a single 2,406-bp open reading frame corresponding to the xynD gene. The predicted product has a characteristic signal sequence that is followed by an amino-terminal domain related to family G xylanases, while the carboxy-terminal domain is related to beta(1,3-1,4)-glucanases from several other bacterial species. These two domains are connected by a region of unknown function that consists of 309 amino acids and includes a 30-amino-acid threonine-rich sequence. A polypeptide having a molecular weight of approximately 90,000 and exhibiting xylanase and beta(1,3-1,4)-glucanase activities was detected in Escherichia coli cells carrying the cloned xynD gene. This is one of the first cases in which a microbial polysaccharidase has been shown to carry separate catalytic domains active against different plant cell wall polysaccharides within the same polypeptide. xynD is one of a family of related genes in R. flavefaciens that encode enzymes having multiple catalytic domains, and the amino terminus of XYLD exhibits a high degree of similarity with the corresponding regions of another xylanase, XYLA, which carries two different xylanase catalytic domains.

AB - Adjacent regions of a Ruminococcus flavefaciens 17 DNA fragment were found to encode xylanase and beta(1,3-1,4)-glucanase activities. Sequencing of this fragment showed that both activities are encoded by a single 2,406-bp open reading frame corresponding to the xynD gene. The predicted product has a characteristic signal sequence that is followed by an amino-terminal domain related to family G xylanases, while the carboxy-terminal domain is related to beta(1,3-1,4)-glucanases from several other bacterial species. These two domains are connected by a region of unknown function that consists of 309 amino acids and includes a 30-amino-acid threonine-rich sequence. A polypeptide having a molecular weight of approximately 90,000 and exhibiting xylanase and beta(1,3-1,4)-glucanase activities was detected in Escherichia coli cells carrying the cloned xynD gene. This is one of the first cases in which a microbial polysaccharidase has been shown to carry separate catalytic domains active against different plant cell wall polysaccharides within the same polypeptide. xynD is one of a family of related genes in R. flavefaciens that encode enzymes having multiple catalytic domains, and the amino terminus of XYLD exhibits a high degree of similarity with the corresponding regions of another xylanase, XYLA, which carries two different xylanase catalytic domains.

KW - NUCLEOTIDE-SEQUENCE

KW - MOLECULAR-CLONING

KW - BACILLUS-PUMILUS

KW - BETA-GLUCANASE

KW - DNA-SEQUENCE

KW - EXPRESSION

KW - RUMEN

KW - BACTERIA

KW - SUBTILIS

M3 - Article

VL - 175

SP - 2943

EP - 2951

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 10

ER -