The BioGRID | PUBLICATION VIEW

	Yeast Dec (2006); 23(16):1151-66
In vitro characterization of the Mig1 repressor from Saccharomyces cerevisiae reveals evidence for monomeric and higher molecular weight forms-
Needham PG, Trumbly RJ
Department of Biochemistry and Cancer Biology, University of Toledo College of Medicine, 3035 Arlington Avenue, Toledo, OH 43614, USA-
Abstract: The Mig1 DNA-binding protein of Saccharomyces cerevisiae was expressed and purified from yeast and the physical properties were characterized by several methods, including gel filtration, sucrose gradient sedimentation and native gel electrophoresis- Purified Mig1 exists as a monomer with a Stokes' radius of 48 A and a sedimentation coefficient of 3-55 S- Mig1 has an elongated shape with a frictional coefficient of 1-83- The K-d- of purified Mig1 for the SUC2 A site is 2-8 nM and for SUC2 B site 25-8 nM; these values were similar for Mig1 purified from repressed and derepressed cells- Full-length Mig1 expressed in yeast binds more tightly to SUC2 B than bacterially expressed GST-Mig1- Sucrose gradient sedimentation resolved a larger molecular weight form of Mig1 in whole-cell extracts that was not seen in purified samples and may represent a complex with another protein- This complex is found within the nucleus and is seen only in repressed cells- Mig1 exists in multiple phosphorylation states and only less phosphorylated forms of Mig1 are associated with this complex- Copyright -c- 2006 John Wiley - Sons, Ltd-
[PUBMED: 17133623]