PMID:11673440
| Citation |
Szeto, TH, Rowland, SL and King, GF (2001) The dimerization function of MinC resides in a structurally autonomous C-terminal domain. J. Bacteriol. 183:6684-7 |
|---|---|
| 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. |
| Links |
PubMed PMC95501 Online version:10.1128/JB.183.22.6684-6687.2001 |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Cell Division; Dimerization; Escherichia coli/cytology; Escherichia coli/metabolism; Mass Spectrometry; Molecular Sequence Data; Peptide Fragments/analysis; Peptide Fragments/chemistry; Proline; Sequence Analysis, Protein |
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