title: The dimerization function of MinC resides in a structurally autonomous C-terminal domain.
abstract: Limited proteolysis of the Escherichia coli cell division inhibitor MinC reveals that its dimerization function resides in a structurally autonomous C-terminal domain. We show that cytoplasmic MinC is poised near the monomer-dimer equilibrium and propose that it only becomes entirely dimeric once recruited to the membrane by MinD.
authors.affiliation: Department of Biochemistry, University of Connecticut Health Center, Framington 06032, USA.
authors.forename: T H
authors.initials: TH
authors.lastname: Szeto
authors.forename: S L
authors.initials: SL
authors.lastname: Rowland
authors.forename: G F
authors.initials: GF
authors.lastname: King
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D002455:Cell Division; D019281:Dimerization; D004926:Escherichia coli / Q000166:cytology / Q000378:metabolism*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis / Q000737:chemistry; D011392:Proline; D020539:Sequence Analysis, Protein
chemical_list: D001426:Bacterial Proteins; C080466:MinC protein, Bacteria; D010446:Peptide Fragments; D011392:Proline