title: Isolation, characterization and lipid-binding properties of the recalcitrant FtsA division protein from Escherichia coli.
abstract: 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 FtsA is folded, mostly monomeric and interacts with lipids. The apparent affinity of FtsA binding to the inner membrane is ten-fold higher than to phospholipids, suggesting that inner membrane proteins could modulate FtsA-membrane interactions. Binding of FtsA to lipids and membranes is insensitive to ionic strength, indicating that a net contribution of hydrophobic interactions is involved in the association of FtsA to lipid/membrane structures.
authors: Centro de Investigaciones Biológicas-CSIC, Madrid, Spain.
authors: Ariadna
authors: A
authors: Martos
authors: Begoña
authors: B
authors: Monterroso
authors: Silvia
authors: S
authors: Zorrilla
authors: Belén
authors: B
authors: Reija
authors: Carlos
authors: C
authors: Alfonso
authors: Jesús
authors: J
authors: Mingorance
authors: Germán
authors: G
authors: Rivas
authors: Mercedes
authors: M
authors: Jiménez
mesh_terms: D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D029968:Escherichia coli Proteins / Q000302:isolation & purification* / Q000378:metabolism; D050356:Lipid Metabolism; D011485:Protein Binding; D017510:Protein Folding; D013056:Spectrophotometry, Ultraviolet
chemical_list: D029968:Escherichia coli Proteins; C489310:FtsA protein, E coli