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- Eklund, MalinKTH,Bioteknologi (author)
Site-specific and reversible anchoring of active proteins onto cellulose using a cellulosome-like complex
- Article/chapterEnglish2004
Publisher, publication year, extent ...
- Elsevier BV,2004
- printrdacarrier
Numbers
- LIBRIS-ID:oai:DiVA.org:kth-23499
- https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-23499URI
- https://doi.org/10.1016/j.jbiotec.2004.01.008DOI
Supplementary language notes
- Language:English
- Summary in:English
Part of subdatabase
- SwePubSwePub
Classification
Notes
- QC 20100525
- Protein engineering strategies facilitating controlled and spontaneous assembly of macromolecular complexes are of great interest for the design of artificial multi-enzyme systems of pre-defined composition. Here we have combined affinity proteins from different sources to achieve specific and reversible anchoring of affinity domain-tagged reporter proteins to a cell ulose-anchored fusion protein. The design principle mimics the architecture of macromolecular cellulosome complexes produced by some cellulolytic microbes. A fusion protein between a cellulose-binding module (CBM1(Cel6A)) of the Trichoderma reesei cellobiohydrolase Cel6A and a five-domain staphylococcal protein A (SPA) was constructed to serve as platform for docking of easily detectable reporter proteins onto cellulose surfaces. In turn, the reporter proteins were produced as fusions to two copies of a SPA-binding affinity protein (an affibody denoted Z(SPA-1)), selected from a phage display library constructed by combinatorial protein engineering. In a series of experiments, involving repeated washing and low pH elution, affinity-tagged Enhanced Green Fluorescent Protein (EGFP) and Fusarium solani pisi lipase cutinase reporter proteins were both found to be specifically directed from solution to the same region of a cellulose filter paper where SPA-CBM1(Cel6A) fusion protein had been previously applied. This showed that the SPA-CBM1(Cel6A) fusion protein had been stably anchored to the cellulose surface without loss of binding capacity and that the interaction between SPA and the Z(SPA-1) affibody domains was selective. The generality of this biospecificity-driven system for assembly applications is discussed.
Subject headings and genre
- NATURVETENSKAP Biologi hsv//swe
- NATURAL SCIENCES Biological Sciences hsv//eng
- cellulosome
- assembly
- affibody
- affinity gene fusion
- protein engineering
- cellulose
- bacterial receptor domain
- binding domain
- combinatorial library
- degradation
- expression
- machines
- affibody
- chimeras
- peptides
- systems
Added entries (persons, corporate bodies, meetings, titles ...)
- Sandström, KristoferKTH,Bioteknologi(Swepub:kth)u1qc3vv1 (author)
- Teeri, TuulaKTH,Bioteknologi(Swepub:kth)u1vcejiv (author)
- Nygren, Per-ÅkeKTH,Bioteknologi(Swepub:kth)u1zhverl (author)
- KTHBioteknologi (creator_code:org_t)
Related titles
- In:Journal of Biotechnology: Elsevier BV109:3, s. 277-2860168-16561873-4863
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- Royal Institute of Technology
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