Cargando…
Isolation, Characterization and Lipid-Binding Properties of the Recalcitrant FtsA Division Protein from Escherichia coli
We have obtained milligram amounts of highly pure Escherichia coli division protein FtsA from inclusion bodies with an optimized purification method that, by overcoming the reluctance of FtsA to be purified, surmounts a bottleneck for the analysis of the molecular basis of FtsA function. Purified Ft...
Autores principales: | Martos, Ariadna, Monterroso, Begoña, Zorrilla, Silvia, Reija, Belén, Alfonso, Carlos, Mingorance, Jesús, Rivas, Germán, Jiménez, Mercedes |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3384640/ https://www.ncbi.nlm.nih.gov/pubmed/22761913 http://dx.doi.org/10.1371/journal.pone.0039829 |
Ejemplares similares
-
Charged Molecules Modulate the Volume Exclusion Effects Exerted by Crowders on FtsZ Polymerization
por: Monterroso, Begoña, et al.
Publicado: (2016) -
Assembly and architecture of Escherichia coli divisome proteins FtsA and FtsZ
por: Morrison, Josiah J., et al.
Publicado: (2022) -
The Nucleoid Occlusion SlmA Protein Accelerates the Disassembly of the FtsZ Protein Polymers without Affecting Their GTPase Activity
por: Cabré, Elisa J., et al.
Publicado: (2015) -
Role of the FtsA C Terminus as a Switch for Polymerization and Membrane Association
por: Krupka, Marcin, et al.
Publicado: (2014) -
Escherichia coli FtsA forms lipid-bound minirings that antagonize lateral interactions between FtsZ protofilaments
por: Krupka, Marcin, et al.
Publicado: (2017)