This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Szeto, J. Articles by Dillon, J.-A. R. Search for Related Content PubMed PubMed Citation Articles by Szeto, J. Articles by Dillon, J.-A. R.

The N Terminus of MinD Contains Determinants Which Affect Its Dynamic Localization and Enzymatic Activity

Department of Biochemistry, Microbiology, and Immunology,¹ Centre for Research in Biopharmaceuticals University of Ottawa, Ottawa, Ontario, Canada²

Received 19 February 2004/ Accepted 30 July 2004

MinD is involved in regulating the proper placement of the cytokinetic machinery in some bacteria, including Neisseria gonorrhoeae and Escherichia coli. Stimulation of the ATPase activity of MinD by MinE has been proposed to induce dynamic, pole-to-pole oscillations of MinD in E. coli. Here, we investigated the effects of deleting or mutating conserved residues within the N terminus of N. gonorrhoeae MinD (MinD_Ng) on protein dynamism, localization, and interactions with MinD_Ng and with MinE_Ng. Deletions or mutations were generated in the first five residues of MinD_Ng, and mutant proteins were evaluated by several functional assays. Truncation or mutation of N-terminal residues disrupted MinD_Ng interactions with itself and with MinE. Although the majority of green fluorescent protein (GFP)-MinD_Ng mutants could still oscillate from pole to pole in E. coli, the GFP-MinD_Ng oscillation cycles were significantly faster and were accompanied by increased cytoplasmic localization. Interestingly, in vitro ATPase assays indicated that MinD_Ng proteins lacking the first three residues or with an I5E substitution possessed higher MinE_Ng-independent ATPase activities than the wild-type protein. These results indicate that determinants found within the extreme N terminus of MinD_Ng are implicated in regulating the enzymatic activity and dynamic localization of the protein.

This article has been cited by other articles:

• Rigden, M. D., Baier, C., Ramirez-Arcos, S., Liao, M., Wang, M., Dillon, J.-A. R. (2008). Identification of the Coiled-coil Domains of Enterococcus faecalis DivIVA that Mediate Oligomerization and their Importance for Biological Function. J Biochem 144: 63-76 [Abstract] [Full Text]