ParM
ParM is a protein that plays a crucial role in the plasmid segregation process in bacteria. It is part of the ParABS system, which is a widely conserved mechanism for DNA segregation and cell division in prokaryotes. ParM is an actin-like protein, meaning it shares structural and functional similarities with eukaryotic actin, a protein essential for maintaining cell shape, mobility, and division.
Structure[edit | edit source]
ParM exhibits a dynamic filamentous structure, capable of rapid polymerization and depolymerization, which is essential for its role in plasmid segregation. The protein forms rigid, double-helical filaments that can push plasmids to opposite poles of the cell before cytokinesis, ensuring equal distribution of genetic material between daughter cells.
Function[edit | edit source]
The primary function of ParM is to mediate the active segregation of R plasmids, a type of plasmid carrying antibiotic resistance genes. It achieves this by assembling into filaments that elongate between two copies of a plasmid, pushing them towards opposite ends of the cell. This mechanism is ATP-dependent, requiring energy for the polymerization of ParM filaments.
Mechanism[edit | edit source]
The segregation process begins with the binding of ParM to the ParR protein, which is attached to the plasmid at a specific sequence known as the parC site. Upon binding ATP, ParM polymerizes into filaments. As more ParM monomers add to the filament, it exerts a pushing force that segregates the plasmids. After the plasmids are moved to the cell poles, ParM filaments depolymerize, allowing the cell to proceed with cytokinesis.
Clinical Significance[edit | edit source]
Understanding the mechanism of ParM-mediated plasmid segregation can provide insights into the spread of antibiotic resistance among bacterial populations. Targeting the ParM system could offer a novel approach to combating antibiotic-resistant infections by preventing the distribution of resistance genes.
See Also[edit | edit source]
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