Microbial production of spider silk proteins.
The remarkable properties of spider dragline silk and related protein polymers will find many applications if the materials can be produced economically. We have demonstrated the production of high molecular weight spider dragline silk analog proteins encoded by synthetic genes in several microbial systems, including Escherichia coli and Pichia pastoris. In E. coli, proteins of up to 1000 amino acids in length could be produced efficiently, but the yield and homogeneity of higher molecular weight silk proteins were found to be limited by truncated synthesis, probably as a result of ribosome termination errors. No such phenomenon was observed in the yeast P. pastoris, where higher molecular weight silk proteins could be produced without heterogeneity due to truncated synthesis. Spider dragline silk analog proteins could be secreted by P. pastoris when fused to both the signal sequence and N-terminal pro-sequence of the Saccharomyces cerevisiae alpha-mating factor gene.
Fahnestock
S R
SR
DuPont Experimental Station, DuPont Central Research and Development, P.O. Box 80328, Wilmington, DE 19880-0328, USA. stephen.fahnestock@usa.dupont.com
Yao
Z
Z
Bedzyk
L A
LA
D000595:Amino Acid Sequence; D000818:Animals; D001709:Biotechnology / Q000379:methods; D003001:Cloning, Molecular; D004926:Escherichia coli; D019476:Insect Proteins / Q000096:biosynthesis* / Q000235:genetics; D008969:Molecular Sequence Data; D030781:Organisms, Genetically Modified; D010843:Pichia; D030821:Plants, Genetically Modified; D011994:Recombinant Proteins; D013112:Spiders / Q000235:genetics*
D019476:Insect Proteins; D011994:Recombinant Proteins