[Cloning, expression and structure of the functionally active shortened lon gene in Escherichia coli].

Klonirovanie, ékspressiia i struktura funktsional'no aktivnogo ukorochennogo gena lon Escherichia coli.

Bioorganicheskaia khimiia ·Vol. 14 ·No. 3 ·1988-03-00 ·Pages 408-11

Amerik AIu, Chistiakov LG, Ostroumova NI, Gurevich AI, Antonov VK

Abstract

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.

MeSH Terms

ATP-Dependent Proteases Amino Acid Sequence Base Sequence Cloning, Molecular Escherichia coli/enzymology,genetics Escherichia coli Proteins Gene Expression Regulation Genes, Bacterial Heat-Shock Proteins Molecular Sequence Data Plasmids Protease La Serine Endopeptidases/genetics

Chemicals

Escherichia coli Proteins Heat-Shock Proteins ATP-Dependent Proteases Serine Endopeptidases Lon protein, E coli Protease La

Authors & Affiliations

5 authors, click to expand affiliations / ORCID

Amerik A Iu

Chistiakov L G

Ostroumova N I

Gurevich A I

Antonov V K

Article Info

Journal

Bioorganicheskaia khimiia

Abbr.

Bioorg Khim

ISSN

0132-3423

Published

1988-03-00

Pages

408-11

Language

rus

Region

Russia (Federation)

NLM ID

7804941

Subset

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[Cloning, expression and structure of the functionally active shortened lon gene in Escherichia coli].

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