Towards deconvoluting the interaction of the Bacillus subtilis sporulation proteins SinR and SinI using tryptophan analogue incorporated proteins

作者: D. J. Scott , S. Leejeerajumnean , J. A. Brannigan , R. J. Lewis , A. J. Wilkinson

DOI: 10.1007/3-540-48703-4_31

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摘要: Sporulation in Bacillus subtilis is used as the strategy of last resort for survival organism and it a very tightly controlled developmental process. One control checkpoints that must be overcome sporulation to occur repression genes by protein SinR (13.5 kDa). This done binding anti-repressor SinI (6.5 kDa) form bound heterodimer. To investigate interaction with solution, an analytical ultracentrifuge study was undertaken. found tetramer, whereas monomer/dimer equilibrium. Derivatives both SinR, where native tryptophan replaced analogue 7-aza-tryptophan (7AW), were expressed active wild-type proteins. The 7AW proteins have property having significant absorbance at 315 nm, thus allowing them monitored even presence containing proteins, making ideal studying protein/protein interactions.

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