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Characterization Of The Interaction Between Ftsz-Ring Stabilizer Zapc And The Conserved Protease Clpxp In E. Coli Cytokinesis, Andrea Cardenas Arevalo
Characterization Of The Interaction Between Ftsz-Ring Stabilizer Zapc And The Conserved Protease Clpxp In E. Coli Cytokinesis, Andrea Cardenas Arevalo
Dissertations and Theses
Cell division in bacteria requires the assembly of a macromolecular protein machinery at midcell that is spatiotemporally regulated during the bacterial cell cycle. Central to the process of division is the assembly of a cytokinetic ring-like structure, termed the Z-ring, formed by polymers of the essential tubulin-homolog FtsZ. Polymerization of FtsZ is regulated by a number of proteins that bind FtsZ and regulate its assembly/disassembly mechanisms. Despite being extensively studied, the molecular nature of the diverse protein-protein interactions that regulate the assembly of FtsZ during early stages of division is not well understood. Here, I focus on an FtsZ-ring stabilizer …
Structure-Function Analysis Of Zapc, An Ftsz-Ring Stabilizer, In Escherichia Coli Cytokinesis, Lukasz Tchorzewski
Structure-Function Analysis Of Zapc, An Ftsz-Ring Stabilizer, In Escherichia Coli Cytokinesis, Lukasz Tchorzewski
Dissertations and Theses
In Escherichia coli, cell division is defined by the polymerization and constriction of a cytokinetic ring (Z ring) formed by FtsZ, a tubulin-like GTPase, at midcell. Division also involves the formation of a multi-protein complex at midcell known as the divisome. Several divisome proteins promote the assembly/disassembly processes of FtsZ, thereby exercising spatiotemporal control over division. Among FtsZ regulatory proteins are the FtsZ ringassociated proteins (Zap), which either directly or indirectly stabilize the Z-ring by increasing lateral interactions amongst FtsZ protofilaments in the Z-ring. ZapA-D are recruited during early cytokinesis and have overlapping functions in stabilizing FtsZ at midcell, but …