THE NUCLEOTIDE-SEQUENCE OF THE BETA-GLUCOSIDASE GENE FROM CELLVIBRIO-GILVUS

被引:16
作者
KASHIWAGI, Y
AOYAGI, C
SASAKI, T
TANIGUCHI, H
机构
[1] National Food Research Institute, Ministry of Agriculture, Tsukuba, Ibaraki, 305, Forestry and Fisheries, 2-1-2, Kannondai
来源
JOURNAL OF FERMENTATION AND BIOENGINEERING | 1993年 / 75卷 / 03期
关键词
D O I
10.1016/0922-338X(93)90108-K
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
A gene encoding beta-glucosidase from Cellvibrio gilvus, a cellobiose-producing bacterium, was cloned into Escherichia coli and sequenced. The structural gene consisted of 2565 bp encoding 854 amino acid residues with a characteristic signal peptide. A typical promoter sequence and SD region were located upstream of the initiation ATG codon. A sequence (180 amino acids) having high homology with those of beta-glucosidases from several microorganisms was found in the deduced amino acid sequence of C. gilvus beta-glucosidase. This sequence contains the aspartic acid residue which was found to be an active site residue in Aspergillus wentii beta-glucosidase A3. The beta-glucosidase gene of C. gilvus contains a high amount (69.4%) of G + C. These bases are localized not in the 3rd position of the codon, as is usually observed in G + C-rich genes, but rather in the lst position. This result in a peptide which contains an extremely high amount (48%) of four amino acids (Pro, Ala, Arg, Gly) coded by CCN, GCN, CGN, and GGN.
引用
收藏
页码:159 / 165
页数:7
相关论文
共 30 条
[1]   ISOLATION AND STRUCTURE OF A TRYPTIC GLYCOPEPTIDE FROM THE ACTIVE-SITE OF BETA-GLUCOSIDASE A3 FROM ASPERGILLUS-WENTII [J].
BAUSE, E ;
LEGLER, G .
BIOCHIMICA ET BIOPHYSICA ACTA, 1980, 626 (02) :459-465
[2]   MOLECULAR-BIOLOGY OF CELLULOSE DEGRADATION [J].
BEGUIN, P .
ANNUAL REVIEW OF MICROBIOLOGY, 1990, 44 :219-248
[3]   THE RELATIONSHIP BETWEEN BASE COMPOSITION AND CODON USAGE IN BACTERIAL GENES AND ITS USE FOR THE SIMPLE AND RELIABLE IDENTIFICATION OF PROTEIN-CODING SEQUENCES [J].
BIBB, MJ ;
FINDLAY, PR ;
JOHNSON, MW .
GENE, 1984, 30 (1-3) :157-166
[4]   A TECHNIQUE FOR RADIOLABELING DNA RESTRICTION ENDONUCLEASE FRAGMENTS TO HIGH SPECIFIC ACTIVITY [J].
FEINBERG, AP ;
VOGELSTEIN, B .
ANALYTICAL BIOCHEMISTRY, 1983, 132 (01) :6-13
[5]   STRUCTURE OF THE BETA-GLUCOSIDASE GENE BGLA OF CLOSTRIDIUM-THERMOCELLUM - SEQUENCE-ANALYSIS REVEALS A SUPERFAMILY OF CELLULASES AND BETA-GLYCOSIDASES INCLUDING HUMAN LACTASE PHLORIZIN HYDROLASE [J].
GRABNITZ, F ;
SEISS, M ;
RUCKNAGEL, KP ;
STAUDENBAUER, WL .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1991, 200 (02) :301-309
[6]  
GREBNITZ F, 1989, MOL GEN GENET, V217, P70
[7]   PURIFICATION AND PROPERTIES OF A XYLANASE FROM CELLVIBRIO-GILVUS THAT HYDROLYZES PARA-NITROPHENYL CELLOOLIGOSACCHARIDES [J].
HAGA, K ;
KITAOKA, M ;
KASHIWAGI, Y ;
SASAKI, T ;
TANIGUCHI, H .
AGRICULTURAL AND BIOLOGICAL CHEMISTRY, 1991, 55 (08) :1959-1967
[8]   DISACCHARIDE PREFERENCE OF AN AEROBIC CELLULOLYTIC BACTERIUM, CELLVIBRIO-GILVUS N SP [J].
HULCHER, FH ;
KING, KW .
JOURNAL OF BACTERIOLOGY, 1958, 76 (06) :565-570
[10]   CHARACTERIZATION OF A BETA-GLUCOSIDASE ENCODED BY A GENE FROM CELLVIBRIO-GILVUS [J].
KASHIWAGI, Y ;
IIJIMA, C ;
SASAKI, T ;
TANIGUCHI, H .
AGRICULTURAL AND BIOLOGICAL CHEMISTRY, 1991, 55 (10) :2553-2559