About: MINC is a research topic. Over the lifetime, 103 publications have been published within this topic receiving 5045 citations. The topic is also known as: MINC is not C.
TL;DR: In this paper, a multiple interacting continua method (MINC) is proposed for numerical simulation of heat and multi-phase fluid flow in multidimensional, fractured porous media.
Abstract: A Multiple Interacting Continua method (MINC) is presented which is applicable for numerical simulation of heat and multi-phase fluid flow in multidimensional, fractured porous media. This method is a generalization of the double-porosity concept. The partitioning of the flow domain into computational volume elements is based on the criterion of approximate thermodynamic equilibrium at all times within each element. The thermodynamic conditions in the rock matrix are assumed to be primarily controlled by the distance from the fractures, which leads to the use of nested grid blocks. The MINC concept is implemented through the Integral Finite Difference (IFD) method. No analytical approximations are made for the coupling between the fracture and matrix continua. Instead, the transient flow of fluid and heat between matrix and fractures is treated by a numerical method. The geometric parameters needed in a simulation are preprocessed from a specification of fracture spacings and apertures, and the geometry of the matrix blocks. The MINC method is verified by comparison with the analytical solution of Warren and Root. Illustrative applications are given for several geothermal reservoir engineering problems.
TL;DR: It is found that GFP–MinC is a cytoplasmic protein in the absence of the other Min proteins, and that it is in position to inhibit Z ring assembly away from midcell.
Abstract: Placement of the Z ring at midcell in Escherichia coli is assured by the action of the min system, which blocks usage of potential division sites that exist at the cell poles. This activity of min is achieved through the action of an inhibitor of division, MinC, that is activated by MinD and topologically regulated by MinE. In this study, we have used a functional GFP-MinC fusion to monitor the location of MinC. We find that GFP-MinC is a cytoplasmic protein in the absence of the other Min proteins. The addition of MinD, a peripheral membrane protein that interacts with MinC, results in GFP-MinC appearing on the membrane. In the presence of both MinD and MinE, GFP-MinC oscillates rapidly between the halves of the cell. Thus, MinC is positioned by the other Min products, but in a dynamic manner so that it is in position to inhibit Z ring assembly away from midcell.
TL;DR: Functional green fluorescent protein-MinC displays a very similar oscillatory behavior which is dependent on both MinD and MinE and independent of FtsZ, and support a model in which MinD recruits MinC to its site of action and in which FTSZ ring assembly at each of the cell ends is blocked in an intermittent and alternate fashion.
Abstract: By inhibiting FtsZ ring formation near the cell ends, the MinC protein plays a critical role in proper positioning of the division apparatus in Escherichia coli. MinC activity requires that of MinD, and the MinE peptide provides topological specificity by suppressing MinC-MinD-mediated division inhibition specifically at the middle of the cell. We recently presented evidence that MinE not only accumulates in an FtsZ-independent ring structure at the cell’s middle but also imposes a unique dynamic localization pattern upon MinD in which the latter accumulates alternately in either one of the cell halves in what appears to be a rapidly oscillating membrane association-dissociation cycle. Here we show that functional green fluorescent protein-MinC displays a very similar oscillatory behavior which is dependent on both MinD and MinE and independent of FtsZ. The results support a model in which MinD recruits MinC to its site of action and in which FtsZ ring assembly at each of the cell ends is blocked in an intermittent and alternate fashion.
TL;DR: It is suggested that MinC rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings.
Abstract: Positioning of the Z ring at the midcell site in Escherichia coli is assured by the min system, which masks polar sites through topological regulation of MinC, an inhibitor of division. To study how MinC inhibits division, we have generated a MalE-MinC fusion that retains full biological activity. We find that MalE-MinC interacts with FtsZ and prevents polymerization without inhibiting FtsZ's GTPase activity. MalE-MinC19 has reduced ability to inhibit division, reduced affinity for FtsZ, and reduced ability to inhibit FtsZ polymerization. These results, along with MinC localization, suggest that MinC rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings.
TL;DR: In living cells, MinE undergoes a rapid localization cycle that appears coupled to MinD oscillation, which supports a model in which MinE stimulates the removal of MinD from the membrane in a wave‐like fashion.
Abstract: The MinC protein directs placement of the division septum to the middle of Escherichia coli cells by blocking assembly of the division apparatus at other sites. MinD and MinE regulate MinC activity by modulating its cellular location in a unique fashion. MinD recruits MinC to the membrane, and MinE induces MinC/MinD to oscillate rapidly between the membrane of opposite cell halves. Using fixed cells, we previously found that a MinE-green fluorescent protein fusion accumulated in an annular structure at or near the midcell, as well as along the membrane on only one side of the ring. Here we show that in living cells, MinE undergoes a rapid localization cycle that appears coupled to MinD oscillation. The results show that MinE is not a fixed marker for septal ring assembly. Rather, they support a model in which MinE stimulates the removal of MinD from the membrane in a wave-like fashion. These waves run from a midcell position towards the poles in an alternating sequence such that the time-averaged concentration of division inhibitor is lowest at midcell.