Self-organization of the MinE ring in subcellular Min oscillations

نویسندگان

  • Julien Derr
  • Jason T. Hopper
  • Anirban Sain
  • Andrew D. Rutenberg
چکیده

We model the self-organization of the MinE ring that is observed during subcellular oscillations of the proteins MinD and MinE within the rod-shaped bacterium Escherichia coli. With a steady-state approximation, we can study the MinE-ring generically – apart from the other details of the Min oscillation. Rebinding of MinE to depolymerizing MinD filament tips controls MinE ring formation through a scaled cell shape parameter r̃. We find two types of E-ring profiles near the filament tip: a strong plateau-like E-ring controlled by 1D diffusion of MinE along the bacterial length, or a weak cusp-like E-ring controlled by 3D diffusion near the filament tip. While the width of a strong E-ring depends on r̃, the occupation fraction of MinE at the MinD filament tip is saturated and hence the depolymerization speed do not depend strongly on r̃. Conversely, for weak E-rings both r̃ and the MinE to MinD stoichiometry strongly control the tip occupation and hence the depolymerization speed. MinE rings in vivo are close to the threshold between weak and strong, and so MinD-filament depolymerization speed should be sensitive to cell shape, stoichiometry, and the MinE-rebinding rate. We also find that the transient to MinE-ring formation is quite long in the appropriate open geometry for assays of ATPase activity in vitro, explaining the long delays of ATPase activity observed for smaller MinE concentrations in those assays without the need to invoke cooperative MinE activity.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Self-organization of the MinE protein ring in subcellular Min oscillations.

We model the self-organization of the MinE ring that is observed during subcellular oscillations of the proteins MinD and MinE within the rod-shaped bacterium Escherichia coli. With a steady-state approximation, we can study the MinE ring generically--apart from the other details of the Min oscillation. Rebinding of MinE to depolymerizing MinD-filament tips controls MinE-ring formation through ...

متن کامل

Pattern formation in Escherichia coli: a model for the pole-to-pole oscillations of Min proteins and the localization of the division site.

Proper cell division requires an accurate definition of the division plane. In bacteria, this plane is determined by a polymeric ring of the FtsZ protein. The site of Z ring assembly in turn is controlled by the Min system, which suppresses FtsZ polymerization at noncentral membrane sites. The Min proteins in Escherichia coli undergo a highly dynamic localization cycle, during which they oscill...

متن کامل

Dynamic structures in Escherichia coli: spontaneous formation of MinE rings and MinD polar zones.

In Escherichia coli, division site selection is regulated in part by the Min-protein system. Oscillations of the Min proteins from pole to pole every approximately 40 sec have been revealed by in vivo studies of GFP fusions. The dynamic oscillatory structures produced by the Min proteins, including a ring of MinE protein, compact polar zones of MinD, and zebra-striped oscillations in filamentou...

متن کامل

Stuttering Min oscillations within E. coli bacteria: a stochastic polymerization model.

We have developed a 3D off-lattice stochastic polymerization model to study the subcellular oscillation of Min proteins in the bacteria Escherichia coli, and used it to investigate the experimental phenomenon of Min oscillation stuttering. Stuttering was affected by the rate of immediate rebinding of MinE released from depolymerizing filament tips (processivity), protection of depolymerizing fi...

متن کامل

Large-scale modulation of reconstituted Min protein patterns and gradients by defined mutations in MinE’s membrane targeting sequence

The E. coli MinDE oscillator is a paradigm for protein self-organization and gradient formation. Previously, we reconstituted Min protein wave patterns on flat membranes as well as gradient-forming pole-to-pole oscillations in cell-shaped PDMS microcompartments. These oscillations appeared to require direct membrane interaction of the ATPase activating protein MinE. However, it remained unclear...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2008