IDENTIFICATION OF NONCATALYTIC CONSERVED REGIONS IN XYLANASES ENCODED BY THE XYNB AND XYND GENES OF THE CELLULOLYTIC RUMEN ANAEROBE RUMINOCOCCUS-FLAVEFACIENS

被引:24
作者
ZHANG, JX [1 ]
MARTIN, J [1 ]
FLINT, HJ [1 ]
机构
[1] ROWETT RES INST,BUCKSBURN AB2 9SB,ABERDEEN,SCOTLAND
来源
MOLECULAR & GENERAL GENETICS | 1994年 / 245卷 / 02期
关键词
XYLANASE; CELLULOLYTIC BACTERIA; ANAEROBIC BACTERIA; RUMINOCOCCUS; SEQUENCE CONSERVATION;
D O I
10.1007/BF00283275
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
xynB is one of at least four genes from the cellulolytic rumen anaerobe Ruminococcus flavefaciens 17 that encode xylanase activity. The xynB gene is predicted to encode a 781-amino acid product starting with a signal peptide, followed by an amino-terminal xylanase domain which is identical at 89% and 78% of residues, respectively, to the amino-terminal xylanase domains of the bifunctional XynD and XynA enzymes from the same organism. Two separate regions within the carboxy-terminal 537 amino acids of XynB also show close similarities with domain B of XynD. These regions show no significant homology with cellulose- or xylan-binding domains from other species, or with any other sequences, and their functions are unknown. In addition a 30 to 32-residue threonine-rich region is present in both XynD and XynB. Codon usage shows a consistent pattern of bias in the three xylanase genes from R. flavefaciens that have been sequenced.
引用
收藏
页码:260 / 264
页数:5
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