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J. Biol. Chem., Vol. 276, Issue 24, 21257-21261, June 15, 2001
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From the Defined chimeric cellulosomes were produced in
which selected enzymes were incorporated in specific locations within a
multicomponent complex. The molecular building blocks of this approach
are based on complementary protein modules from the cellulosomes of two clostridia, Clostridium thermocellum and Clostridium
cellulolyticum, wherein cellulolytic enzymes are incorporated
into the complexes by means of high-affinity species-specific
cohesin-dockerin interactions. To construct the desired complexes, a
series of chimeric scaffoldins was prepared by recombinant means. The
scaffoldin chimeras were designed to include two cohesin modules from
the different species, optionally connected to a cellulose-binding
domain. The two divergent cohesins exhibited distinct specificities
such that each recognized selectively and bound strongly to its
dockerin counterpart. Using this strategy, appropriate
dockerin-containing enzymes could be assembled precisely and by design
into a desired complex. Compared with the mixture of free cellulases,
the resultant cellulosome chimeras exhibited enhanced synergistic
action on crystalline cellulose.
Design and Production of Active Cellulosome Chimeras
SELECTIVE INCORPORATION OF DOCKERIN-CONTAINING ENZYMES INTO
DEFINED FUNCTIONAL COMPLEXES*
,¶,,
,¶, and
Bioénergétique et
Ingéniérie des Protéines, Centre National de la
Recherche Scientifique, Institut de Biologie Structurale et
Microbiologie-Institut Fédératif de Recherche 1, 13402 Marseille, France, the § Department of Biological Chemistry,
The Weizmann Institute of Science, Rehovot 76100, Israel, the
¶ Université de Provence, 13331 Marseille, France, the
Department of Molecular Microbiology and Biotechnology, Tel Aviv
University, Ramat Aviv 69978, Israel, 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 a contract from the European
Commission (Fourth Framework, Biotechnology Programme, BIO4-97-2303) and by grants from the Israel Science Foundation (administered by the
Israel Academy of Sciences and Humanities, Jerusalem). Additional
support was provided by the Otto Meyerhof Center for Biotechnology,
established by the Minerva Foundation (Munich, Germany), and by 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.
To whom correspondence should be addressed: Dept. of
Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel. Tel.: +972-8-934-2373; Fax: +972-8-946-8256; E-mail:
bfbayer@wicc.weizmann.ac.il.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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