title: [The Effect of Mutations in the Inserted Domain of ATP-Dependent Lon Protease from E. coli on the Enzyme Function].
abstract: ATP-Dependent protease LonA from E. coli (Ec-Lon), belonging to the superfamily of AAA+ proteins, is a key member of the protein quality control system in bacterial cells. Ec-Lon functions as homohexamer and degrades abnormal and defective polypeptides as well as a number of regulatory proteins by the processive mechanism. Ec-Lon subunit includes--the both ATPase and proteolytic components (AAA+ module and P domain) in addition to the unique non-catalytic region formed by the N-terminal (N) and the inserted c-helical (HI(CC)) domains. The mutant forms Lon-R164A, Lon-R192A and Lon-Y294A have been obtained and characterized in order to reveal the role of the HI (CC) domain for the enzyme functioning. C-Terminal part of the HI (CC) domain is shown to display an allosteric effect on the efficiency of the enzyme ATPase and proteolytic sites while its coiled-coil (CC) region is involved in the interaction with the protein substrate.
authors.forename: A M
authors.initials: AM
authors.lastname: Kudzhaev
authors.forename: A G
authors.initials: AG
authors.lastname: Andrianova
authors.forename: O V
authors.initials: OV
authors.lastname: Serova
authors.forename: V A
authors.initials: VA
authors.lastname: Arkhipova
authors.forename: E S
authors.initials: ES
authors.lastname: Dubovtseva
authors.forename: T V
authors.initials: TV
authors.lastname: Rotanova
mesh_terms: D002846:Chromatography, Affinity; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics*; D016254:Mutagenesis, Insertional; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D049070:Protease La / Q000737:chemistry* / Q000235:genetics*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D029968:Escherichia coli Proteins; C483567:Lon protein, E coli; D049070:Protease La