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

AUTOR(ES)
FONTE

American Society for Microbiology

RESUMO

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 (MinDNg) on protein dynamism, localization, and interactions with MinDNg and with MinENg. Deletions or mutations were generated in the first five residues of MinDNg, and mutant proteins were evaluated by several functional assays. Truncation or mutation of N-terminal residues disrupted MinDNg interactions with itself and with MinE. Although the majority of green fluorescent protein (GFP)-MinDNg mutants could still oscillate from pole to pole in E. coli, the GFP-MinDNg oscillation cycles were significantly faster and were accompanied by increased cytoplasmic localization. Interestingly, in vitro ATPase assays indicated that MinDNg proteins lacking the first three residues or with an I5E substitution possessed higher MinENg-independent ATPase activities than the wild-type protein. These results indicate that determinants found within the extreme N terminus of MinDNg are implicated in regulating the enzymatic activity and dynamic localization of the protein.

ACESSO AO ARTIGO

Documentos Relacionados