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Expression of a recombinant elastin‐like protein in pichia pastoris
Author(s) -
Sallach Rory E.,
Conticello Vincent P.,
Chaikof Elliot L.
Publication year - 2009
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1002/btpr.208
Subject(s) - pichia pastoris , pentapeptide repeat , recombinant dna , gene , biology , genetics , pichia , sequence (biology) , oligonucleotide , elastin , computational biology , translation (biology) , microbiology and biotechnology , messenger rna , biochemistry , peptide
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. © 2009 American Institute of Chemical Engineers Biotechnol. Prog., 2009
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