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J. Bacteriol., 01 1998, 175-177, Vol 180, No. 1
Copyright © 1998, American Society for Microbiology

Stability of the Escherichia coli division inhibitor protein MinC requires determinants in the carboxy-terminal region of the protein [In Process Citation]

M Sen and LI Rothfield
Department of Microbiology, University of Connecticut Health Center, Farmington 06032, USA.

Certain mutations in the C-terminal region of the Escherichia coli division inhibitor protein MinC cause loss of function of the division inhibitor by making MinC more sensitive to degradation by Lon protease, implying a possible role for the C-terminal region in regulating the stability and cellular concentration of MinC.


This article has been cited by other articles:

  • Zhou, H., Lutkenhaus, J. (2005). MinC Mutants Deficient in MinD- and DicB-Mediated Cell Division Inhibition Due to Loss of Interaction with MinD, DicB, or a Septal Component. J. Bacteriol. 187: 2846-2857 [Abstract] [Full Text]  
  • Ramirez-Arcos, S., Greco, V., Douglas, H., Tessier, D., Fan, D., Szeto, J., Wang, J., Dillon, J. R. (2004). Conserved Glycines in the C Terminus of MinC Proteins Are Implicated in Their Functionality as Cell Division Inhibitors. J. Bacteriol. 186: 2841-2855 [Abstract] [Full Text]  
  • Johnson, J. E., Lackner, L. L., de Boer, P. A. J. (2002). Targeting of DMinC/MinD and DMinC/DicB Complexes to Septal Rings in Escherichia coli Suggests a Multistep Mechanism for MinC-Mediated Destruction of Nascent FtsZ Rings. J. Bacteriol. 184: 2951-2962 [Abstract] [Full Text]  
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  • Herman, C., Thévenet, D., Bouloc, P., Walker, G. C., D'Ari, R. (1998). Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH). Genes Dev. 12: 1348-1355 [Abstract] [Full Text]  


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