[Cloning, expression and structure of the functionally active shortened lon gene in Escherichia coli].
Lon gene of E. coli has been cloned into the plasmid pBR327. Full nucleotide sequence of the gene has been established. It was shown that the cloned gene does not possess the terminal codon and is somewhat shortened. Nevertheless it retains full phenotypic activity and expresses the C-end modified La proteinase which retains ATP-dependent proteolytic activity.
Amerik
A Iu
AIu
Chistiakov
L G
LG
Ostroumova
N I
NI
Gurevich
A I
AI
Antonov
V K
VK
D049069:ATP-Dependent Proteases; D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D029968:Escherichia coli Proteins; D005786:Gene Expression Regulation; D005798:Genes, Bacterial; D006360:Heat-Shock Proteins; D008969:Molecular Sequence Data; D010957:Plasmids; D049070:Protease La; D012697:Serine Endopeptidases / Q000235:genetics*
D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; C483567:Lon protein, E coli; D049070:Protease La
Klonirovanie, ékspressiia i struktura funktsional'no aktivnogo ukorochennogo gena lon Escherichia coli.