Interactions and Synergism between the Recombinant CelD, an Endoglucanase, and the Cellulosome-Integrating Protein(CipA) of Clostridium thermocellum

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概要

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• The Clostridium thermocellum cellulosome is a multicomponent cellulase complex. Its largest subunit, CipA, contains nine repeated domains (R's), each of which binds to a cellulosomal catalytic subunit, and a cellulose binding domain (CBD). We have previously reported that the activity of CelS, an exoglucanase subunit, is enhanced by the anchorage function of CipA. In this work, we examined the effect of anchorage on the activity of CelD, an endoglucanase subunit, using recombinant CelD (rCelD) and the CipA functional domains, R3 (a repeat next to CBD) and CBD/R3,expressed in Escherichia coli. rCelD formed a stable complex with CBD/R3 as analyzed by a gel-shift assay on a nondenaturing polyacrylamide gradient gel. Binding of rCelD to crystalline cellulose, as its activity toward both phosphoric acid-swollen and crystalline cellulose, was dependent on CBD/R3. These results indicate that the activity of an endoglucanase subunit of the cellulosome, as that of the exoglucanase subunit, is enhanced by the anchorage function of CipA. Such anchorage function of CipA may thus augment the potential endo-exo synergism in the cellulosome.

• 公益社団法人日本生物工学会の論文
• 1997-02-25

著者

• Fukumura Masayuki

  (present Address)dna Vec

• Wu J.h.david

  University Of Rochester Department Of Chemical Engineering

• BEGUM ANWARA

  University of Rochester, Department of Chemical Engineering

• KRUUS KRISTIINA

  (Present address)Genecor International B.V.,

• Kruus Kristiina

  (present Address)genecor International B.v.

• Begum Anwara

  University Of Rochester Department Of Chemical Engineering

関連論文

• Interactions and Synergism between the Recombinant CelD, an Endoglucanase, and the Cellulosome-Integrating Protein(CipA) of Clostridium thermocellum

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