Directed evolution of proteins for heterologous expression and stability.
Recent developments have been made in the application of directed evolution to achieve the efficient heterologous expression of proteins in Escherichia coli and yeast by increasing the stability and solubility of the protein in the host environment. One interesting conclusion that emerges is that the evolutionary process often improves the stability and solubility of an intermediate (apoprotein, proprotein or folding intermediate) that otherwise constitutes a bottleneck to functional expression, rather than altering the protein's final state.
Roodveldt
Cintia
C
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
Aharoni
Amir
A
Tawfik
Dan S
DS
D003001:Cloning, Molecular / Q000379:methods; D019020:Directed Molecular Evolution / Q000379:methods*; D004926:Escherichia coli / Q000502:physiology*; D019143:Evolution, Molecular; D005786:Gene Expression Regulation / Q000502:physiology*; D024861:Genetic Enhancement / Q000379:methods; D015202:Protein Engineering / Q000379:methods*; D011506:Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D011994:Recombinant Proteins / Q000096:biosynthesis; D012441:Saccharomyces cerevisiae / Q000502:physiology*; D012995:Solubility
D011506:Proteins; D011994:Recombinant Proteins