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Quaternary re-arrangement analysed by spectral enhancement: the interaction of a sporulation repressor with its antagonist.

Abstract：

:The protein/protein interaction between SinI and SinR has been studied by analytical ultracentrifugation and gel electrophoresis in an attempt to understand how these proteins contribute to developmental control of sporulation in Bacillus subtilis. SinR was found to be tetrameric, while SinI was found to exist as monomers and dimers in a rapidly reversible equilibrium. Labelling of SinR by incorporating the tryptophan analogue 7-azatryptophan (7AW) into the protein in place of tryptophan shifts the UV absorbance spectrum, thus allowing selective monitoring of 7AWSinR at 315 nm using the UV absorption optics of the analytical ultracentrifuge. Selective monitoring of SinR in mixtures of SinR and SinI enables the binding and stoichiometry of the interaction to be investigated quantitatively and unambiguously. We demonstrate that the oligomeric forms of SinR and SinI re-arrange to form a tight 1:1 SinR:SinI complex, with no stable intermediate species. A fragment of SinR, SinR(1-69), which contains only the DNA-binding domain, was found to be monomeric, showing that the protein appears not to oligomerise in a similar manner to the Cro repressor, a protein with which it shares a marked structural similarity.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Scott DJ,Leejeerajumnean S,Brannigan JA,Lewis RJ,Wilkinson AJ,Hoggett JG

doi

10.1006/jmbi.1999.3221

keywords:

subject

Has Abstract

pub_date

1999-11-12 00:00:00

pages

997-1004

issue

5

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(99)93221-7

journal_volume

293

pub_type

杂志文章

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