[1] Purification of recombinant Rho/Rac/G25K from Escherichia coli
作者： Annette J. Self , Alan Hall
DOI: 10.1016/0076-6879(95)56003-3
关键词: Spodoptera 、 RhoG 、 Biochemistry 、 GTPase 、 RHOA 、 Recombinant DNA 、 Escherichia coli 、 Peptide sequence 、 Guanine nucleotide exchange factor 、 Biology
摘要: Publisher Summary This chapter discusses the purification method of recombinant Rho/Rac/G25K from Escherichia coli . The Ras-related GTP-binding proteins sources has proved to be invaluable for studying their biochemical properties and biological effects. simplest expression systems have made use , although Ras-like GTPases produced in this way are not posttranslationally modified. Yeast baculovirus-Sf9 ( Spodoptera frugiperda fall armyworm ovary) insect cells also been used, because they eukaryotic hosts, expressed at least partially mammalian Rho subfamily consists RhoA, B, C; Rac1l 2; G25K/CDC42; RhoG; TC10. These 30% identical Ras amino acid sequence 55% each other, overall three-dimensional structure is similar that Ras. Like all small GTPases, Rho-related regulated by guanine nucleotide exchange factors (GEFs) GTPase-activating (GAPs), characterization these regulatory relies on a source protein.
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