Local Self-Enhancement of MinD Membrane Binding in min Protein Pattern Formation

Journal of Molecular Biology
Tamara HeermannPetra Schwille


The proteins MinD, MinE and MinC are constitutive for the spatiotemporal organization of cell division in E. coli, in particular, for positioning the division machinery at mid-cell. To achieve this function, the ATPase MinD and the ATPase-activating protein MinE undergo coordinated pole-to-pole oscillations, and have thus become a paradigm for protein pattern formation in biology. The exact molecular mechanisms enabling MinDE self-organization, and particularly the role of cooperativity in the membrane binding of MinD, thought to be a key requirement, have remained poorly understood. However, for bottom-up synthetic biology aiming at a de novo design of key cellular features, elucidating these mechanisms is of great relevance. By combining in vitro reconstitution with rationally-guided mutagenesis of MinD, we found that when bound to membranes, MinD displays new interfaces for multimerization, which are distinct from the canonical MinD dimerization site. We propose that these additional transient interactions contribute to the local self-enhancement of MinD at the membrane, while their relative lability maintains the structural plasticity required for MinDE wave propagation. This could represent a powerful structural regulation...Continue Reading

Related Concepts

Regulation of Biological Process
Mutagenesis Process
Binding (Molecular Function)
MinD protein, Arabidopsis
Lmd protein, Drosophila
Escherichia coli
Up-Regulation (Physiology)

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