Abstract
Self assembly is a prerequisite for fabricating nanoscale structures. Here we present a new fusion protein based on the stress-responsive homo-oligomeric 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.
Original language | American English |
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Pages (from-to) | 433-439 |
Number of pages | 7 |
Journal | Journal of Biotechnology |
Volume | 131 |
Issue number | 4 |
DOIs | |
State | Published - 30 Sep 2007 |
Bibliographical note
Funding Information:This research was supported in part by a grant from the United States–Israel Binational Science Foundation (BSF), Jerusalem, Israel.
Keywords
- Cohesin-dockerin recognition
- Nano-bioreactor
- Nano-fabrication
- SP1
- Scaffold
- Self assembly