The dimerization function of MinC resides in a structurally autonomous C-terminal domain.
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.
Szeto
T H
TH
Department of Biochemistry, University of Connecticut Health Center, Framington 06032, USA.
Rowland
S L
SL
King
G F
GF
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
D001426:Bacterial Proteins; C080466:MinC protein, Bacteria; D010446:Peptide Fragments; D011392:Proline