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Mechanism of the asymmetric activation of the MinD ATPase by MinE
Park, Hyung-Tae Wu, Wei Lovell, Scott Lutkenhaus, Joe
Park, Hyung-Tae
Wu, Wei
Lovell, Scott
Lutkenhaus, Joe
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Abstract
MinD is a component of the Min system involved in the spatial regulation of cell division. It is an ATPase in the MinD/ParA/Mrp deviant Walker A motif family which is within the P loop GTPase superfamily. Its ATPase activity is stimulated by MinE, however, the mechanism of this activation is unclear. MinD forms a symmetric dimer with two binding sites for MinE, however, a recent model suggested that MinE occupying one site was sufficient for ATP hydrolysis. By generating heterodimers with one binding site for MinE we show that one binding site is sufficient for stimulation of the MinD ATPase. Furthermore, comparison of structures of MinD and related proteins led us to examine the role of N45 in the switch I region. An asparagine at this position is conserved in four of the deviant Walker A motif subfamilies (MinD, chromosomal ParAs, Get3 and FleN) and we find that N45 in MinD is essential for MinE stimulated ATPase activity and suggest that it is a key residue affected by MinE binding.
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This is the peer reviewed version of the following article: Park, K.-T., Wu, W., Lovell, S. and Lutkenhaus, J. (2012), Mechanism of the asymmetric activation of the MinD ATPase by MinE. Molecular Microbiology, 85: 271–281. doi:10.1111/j.1365-2958.2012.08110.x, which has been published in final form at http://doi.org/10.1111/j.1365-2958.2012.08110.x. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
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2012-07
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Wiley
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Park, K.-T., Wu, W., Lovell, S. and Lutkenhaus, J. (2012), Mechanism of the asymmetric activation of the MinD ATPase by MinE. Molecular Microbiology, 85: 271–281. doi:10.1111/j.1365-2958.2012.08110.x