Cloning, structure and expression of the full lon gene of Escherichia coli coding for ATP-dependent protease La

A. Yu. Amerik, V. K. Antonov, N. I. Ostroumova, T. V. Rotanova, L. G. Chistyakova

M. M. Shemyakin Institute of Bioorganic Chemistry, Academy of Sciences of the USSR, Moscow

Abstract: Assembly of the full Escherichia coli K-12 lon gene from the EcoRISphI fragment of the bacterial DNA («modified» gene) cloned and sequenced earlier [12]) and the PstI fragment of the same DNA containing 3'-terminal region of the Ion gene has been performed. Both «modified» and full genes showed all phenotype properties of ion gene. The complete nucleotide sequence of the gene (2770 bp) coding for the 784 amino acid sequence of protease La was determined. Location of catalytically active serine, histidine and aspartic acid residues was suggested, and ATP-binding site found. The lon gene and protease La structures we found are compared with those described independently [15] and differences observed are discussed.

Russian Journal of Bioorganic Chemistry 1990, 16 (7):869-880

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