SP1 as a novel scaffold building block for self-assembly nanofabrication of submicron enzymatic structures.
In this study, SP1, a ring-shaped highly stable homododecamer protein complex was utilized for the self-assembly of multiple domains in a predefined manner. Glucose oxidase (GOx) was fused in-frame to SP1 and expressed in Escherichia coli. Complexes where GOx encircled SP1 dodecamer were observed, and moreover, the enzymatic monomers self-assembled into active multienzyme nanotube particles containing hundreds of GOx molecules per tube. This work demonstrates the value of SP1 as a self-assembly scaffold.
Heyman
Arnon
A
The Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, The Hebrew University of Jerusalem, P.O. Box 12, Rehovot 76100, Israel.
Levy
Ilan
I
Altman
Arie
A
Shoseyov
Oded
O
D003460:Crystallization / Q000379:methods; D019281:Dimerization; D029721:Drosophila Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D004800:Enzymes, Immobilized / Q000737:chemistry; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005949:Glucose Oxidase / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure*; D046911:Macromolecular Substances / Q000737:chemistry; D008422:Materials Testing; D008968:Molecular Conformation; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure*; D036103:Nanotechnology / Q000379:methods*; D010316:Particle Size; D015202:Protein Engineering / Q000379:methods; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000648:ultrastructure; D016329:Sp1 Transcription Factor / Q000737:chemistry* / Q000648:ultrastructure*; D013499:Surface Properties
D029721:Drosophila Proteins; D004800:Enzymes, Immobilized; D046911:Macromolecular Substances; D011993:Recombinant Fusion Proteins; D016329:Sp1 Transcription Factor; C403210:Sp1 protein, Drosophila; D005949:Glucose Oxidase