Studies on the Functional Analysis of the Cellulose-binding Protein of the Rumen Cellulolytic Bacterium
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Accession number;04A0022338
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| Title;Studies on the Functional Analysis of the Cellulose-binding Protein of the Rumen Cellulolytic Bacterium |
| Author;
TOYODA ATSUSHI
(Ibaraki Univ., School of Agricuture, JPN)
NAKAMURA YUTAKA
(Ibaraki Univ., School of Agricuture, JPN)
MINATO HAJIME
(Koibuchi Coll. Agriculture, JPN)
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Journal Title;Shokuniku ni kansuru Josei Kenkyu Chosa Seika Hokokusho
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Journal Code:X0296A
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ISSN:
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VOL.21;NO.;PAGE.133-137(2003)
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| Figure&Table&Reference;FIG.4, REF.3 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;Ruminants have developed the ability to digest cellulose by exploiting symbiotic relationship with cellulolytic rumen bacteria. Eubacterium cellulosolvens is one of the predominant cellulolytic bacteria in the rumen. The organism tightly adheres to plant materials and subsequently digests the surface of the materials. In the recent studies, we isolated cellulose-binding proteins from the organism. The 160-kDa protein is major cellulose-binding protein and designated as CBPA. CBPA may be a unique cellulose-binding protein that plays an important role in the adhesion of the bacterium to cellulose. The gene consists of an open reading frame of 3,453 nucleotides and encodes a protein of 1,151 amino acids with a molecular mass of 126,408. The cellulose-binding domain(CBD) of E. cellulosolvens 5 cellulose-binding protein A(CBPA) has been determined. The gene(cbpA) encoding CBPA and its derivatives were expressed in Escherichia coli. We were able to obtain the eight recombinant proteins and examine for the cellulose-binding ability, and carboxymethyl cellulase(CMCase) activity. Since five recombinant proteins, which contain the unknown domain(UD-2) located between two linker-like regions of CBPA, bound to cellulose, this region has been identified as the CBD. The CBD did not show a significant sequence similarity with any other CBDs. Moreover, the N-terminal region of CBPA showed a significant sequence similarity with a catalytic domain of glycosyl hydrolase family 9, and the recombinant proteins containing the region showed CMCase activity. (author abst.) |
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