Comparative fusion expression of maize SINAT5 in two different strains of Escherichia coli

Abstract

SINAT5 is a plant E3 ligase that regulates auxin signaling and root morphogenesis by ubiquitination of the NAC1 protein. Consequently, it may be a putative regulator of aspects of plant development cycles that are controlled by auxin. Efficient production, purification and correctly folded form of this protein are important requirements for functional studies. We produced and quantitatively compared fusion expression of the "maltose binding protein (mbp)-maize sinat5" construct in two different strains of Escherichia coli. One-step purification of fused products gave about 33 mg protein/L bacterial cell culture for E. coli TB1 cells and approximately 18 mg protein/L bacterial cell culture for E. coli DH5α cells. Continuous expression of the fused product and similarity of growth patterns were observed in both cultures.