THE HYDROPHOBIC REPEATED DOMAIN OF THE CLOSTRIDIUM-CELLULOVORANS CELLULOSE-BINDING PROTEIN (CBPA) HAS SPECIFIC INTERACTIONS WITH ENDOGLUCANASES

被引：39

作者：

TAKAGI, M ^{[1
]}

HASHIDA, S ^{[1
]}

GOLDSTEIN, MA ^{[1
]}

DOI, RH ^{[1
]}

机构：

[1] UNIV CALIF DAVIS,DIV BIOL SCI,MOLEC & CELLULAR BIOL SECT,DAVIS,CA 95616

来源：

JOURNAL OF BACTERIOLOGY | 1993年 / 175卷 / 21期

关键词：

D O I：

10.1128/jb.175.21.7119-7122.1993

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

We overexpressed one of the hydrophobic repeated domains (HBDs) (110 amino acid residues) of the cellulose-binding protein (CbpA) from Clostridium cellulovorans by making a hybrid protein with the Escherichia coli maltose-binding protein (MalE). The HBD was purified to homogeneity, and interactions between the HBD and endoglucanases were analyzed by a novel interaction Western blotting (immunoblotting) method. The HBD had specific interactions with endoglucanases (EngB and EngD) from C. cellulovorans. These results indicated that the HBD was an endoglucanase binding site of CbpA.

引用

页码：7119 / 7122

页数：4

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