[Synthesis and characterisation of ATP-dependent forms of Lon-proteinase with modified N-terminal domain from Escherichia coli].
The functional domain boundaries of the ATP-dependent Lon proteases were identified by comparative analysis of the amino acid sequences of the enzymes from evolutionarily distant organisms. Modified forms of the Escherichia coli Lon protease with the elongated or substituted N-terminal domain and a truncated enzyme lacking the N-terminal domain were obtained through genetic engineering methods. Analysis of the enzymatic properties of the resulting modified forms of Lon protease revealed the importance of the N-terminal domain in its function.
Rasulova
F S
FS
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow. fatima@enzyme.siobc.ras.ru
Dergousova
N I
NI
Mel'nikov
E E
EE
Ginodman
L M
LM
Rotanova
T V
TV
D049069:ATP-Dependent Proteases; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D003001:Cloning, Molecular; D017931:DNA Primers; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins; D015870:Gene Expression; D006360:Heat-Shock Proteins / Q000096:biosynthesis* / Q000235:genetics* / Q000302:isolation & purification; D009154:Mutation; D016133:Polymerase Chain Reaction; D049070:Protease La; D015183:Restriction Mapping; D017384:Sequence Deletion; D012697:Serine Endopeptidases / Q000096:biosynthesis* / Q000235:genetics* / Q000302:isolation & purification
D000596:Amino Acids; D017931:DNA Primers; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D000255:Adenosine Triphosphate; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; C483567:Lon protein, E coli; D049070:Protease La
Polucheniie i issledovanie modifitsirovannykh v oblasti N-kontsevogo domena form ATP-zavisimoĭ Lon-proteinazy iz Escherichia coli.