Journal
JOURNAL OF BIOTECHNOLOGY
Volume 131, Issue 4, Pages 433-439Publisher
ELSEVIER
DOI: 10.1016/j.jbiotec.2007.07.940
Keywords
SP1; cohesin-dockerin recognition; self assembly; nano-fabrication; nano-bioreactor; scaffold
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Self assembly is a prerequisite for fabricating nanoscale structures. Here we present a new fusion protein based on the stress-responsive homooligomeric protein, SP1. This ring-shaped protein is a highly stable homododecamer, which can be potentially utilized to self-assemble different modules and enzymes in a predicted and oriented manner. For that purpose, a cohesin module (a component of the bacterial cellulosome) was selected, its gene fused in-frame to SP1, and the fusion protein was expressed in Escherichia coli. The cohesin module, specialized to incorporate different enzymes through specific recognition of a dockerin modular counterpart, is used to display new moieties on the SP1 scaffold. The SP1 scaffold displayed 12 active cohesin modules and specific binding to a dockerin-fused cellulase enzyme from Thermobifida fusca. Moreover, we found a significant increase in specific activity of the scaffold-displayed enzymes. (c) 2007 Elsevier B.V. All rights reserved.
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