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  • Title: In vitro selection of GTP-binding proteins by block shuffling of estrogen-receptor fragments.
    Author: Tsuji T, Onimaru M, Doi N, Miyamoto-Sato E, Takashima H, Yanagawa H.
    Journal: Biochem Biophys Res Commun; 2009 Dec 18; 390(3):689-93. PubMed ID: 19825363.
    Abstract:
    To what extent has alternative splicing contributed to the evolution of protein-function diversity? We previously constructed a pool of block-deletion mutants of the human estrogen receptor alpha ligand binding domain by random multi-recombinant PCR. Here we performed iterative in vitro selection of GTP-binding proteins by using the library of mRNA-displayed proteins and GTP-affinity chromatography combined with quantitative real-time PCR. We obtained a novel GTP-binding protein with moderate affinity and substrate-specificity. The results of our in vitro simulation imply that alternative splicing may have contributed substantially to the diversification of protein function during evolution.
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