Literature DB >> 19827084

Expression of a recombinant elastin-like protein in pichia pastoris.

Rory E Sallach1, Vincent P Conticello, Elliot L Chaikof.   

Abstract

The translation of highly repetitive gene sequences is often associated with reduced levels of protein expression and may be prone to mutational events. In this report, we describe a modified concatemerization strategy to construct a gene with enhanced sequence diversity that encodes a highly repetitive elastin-like protein polymer for expression in Pichia pastoris. Specifically, degenerate oligonucleotides were used to create a monomer library, which after concatemerization yielded a genetically nonrepetitive DNA sequence that encoded identical pentapeptide repeat sequences. By limiting genetic repetition, the risk of genetic deletions, rearrangements, or premature termination errors during protein synthesis is minimized. (c) 2009 American Institute of Chemical Engineers Biotechnol. Prog., 2009.

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Year:  2009        PMID: 19827084      PMCID: PMC2796711          DOI: 10.1002/btpr.208

Source DB:  PubMed          Journal:  Biotechnol Prog        ISSN: 1520-6033


  53 in total

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Review 9.  Self-assembly of block copolymers derived from elastin-mimetic polypeptide sequences.

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  16 in total

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9.  Elastomeric Recombinant Protein-based Biomaterials.

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Review 10.  Applications of elastin-like polypeptides in drug delivery.

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