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J. Biol. Chem., Vol. 277, Issue 51, 49621-49630, December 20, 2002
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From the A library of 75 different chimeric cellulosomes
was constructed as an extension of our previously described approach
for the production of model functional complexes (Fierobe, H.-P.,
Mechaly, A., Tardif, C., Bélaïch, A., Lamed, R., Shoham,
Y., Bélaïch, J.-P., and Bayer, E. A. (2001)
J. Biol. Chem. 276, 21257-21261), based on the high
affinity species-specific cohesin-dockerin interaction. Each complex
contained three protein components: (i) a chimeric scaffoldin
possessing an optional cellulose-binding module and two cohesins of
divergent specificity, and (ii) two cellulases, each bearing a dockerin
complementary to one of the divergent cohesins. The activities of the
resultant ternary complexes were assayed using different types of
cellulose substrates. Organization of cellulolytic enzymes into
cellulosome chimeras resulted in characteristically high activities on
recalcitrant substrates, whereas the cellulosome chimeras showed little
or no advantage over free enzyme systems on tractable substrates. On
recalcitrant cellulose, the presence of a cellulose-binding domain on
the scaffoldin and enzyme proximity on the resultant complex
contributed almost equally to their elevated action on the substrate.
For certain enzyme pairs, however, one effect appeared to predominate
over the other. The results also indicate that substrate recalcitrance is not necessarily a function of its crystallinity but reflects the
overall accessibility of reactive sites.
Degradation of Cellulose Substrates by Cellulosome Chimeras
SUBSTRATE TARGETING VERSUS PROXIMITY OF ENZYME
COMPONENTS*
§,
,,,
Bioénergétique et
Ingéniérie des Protéines, CNRS, IBSM,
13402 Marseille, France, the ¶ Department of Biological
Chemistry, The Weizmann Institute of Science,
Rehovot 76100, Israel, the Université de Provence,
13331 Marseille, the ** Architecture Fonctionnelle des
Macromolécules, CNRS, IBSM, 13402 Marseille, France, the
Department of Molecular Microbiology and
Biotechnology, Tel Aviv University, Ramat Aviv 69978, and the
§§ Department of Food Engineering and
Biotechnology, and Institute of Catalysis Science and Technology,
Technion-Israel Institute of Technology, Haifa 32000, Israel
*
This work was supported by the CNRS, the Conseil
Général des Bouches du Rhône, the Region
Provence-Alpes-Côte d'Azur, the Israel Science Foundation Grants
771/01, 446/01, and 250/99, the Otto Meyerhof Center for Biotechnology
(established by the Minerva Foundation, Munich, Germany), and funds
from the Technion-Niedersachsen Cooperation (Hannover, Germany).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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