Current Microbiology

, Volume 43, Issue 4, pp 260–264

Cloning, Characterization, and Functional Expression in Escherichia coli of argH Encoding Argininosuccinate Lyase in the Cyanobacterium Nostoc sp. Strain PCC 73102

  • Olga Troshina
  • Alfred Hansel
  • Peter Lindblad

DOI: 10.1007/s002840010298

Cite this article as:
Troshina, O., Hansel, A. & Lindblad, P. Curr Microbiol (2001) 43: 260. doi:10.1007/s002840010298

Abstract

A gene argH, encoding argininosuccinate lyase (ASL), has been cloned from a cosmid library of the filamentous cyanobacterium Nostoc sp. strain PCC 73102. The argH open reading frame encodes a protein comprised of 461 amino acids with a calculated molecular mass of 51,349 Da. Protein sequence comparisons reveal significant similarities of the Nostoc PCC 73102 ASL to related proteins from other organisms. In an Escherichia coliΔargH strain, the Nostoc PCC 73102 ASL expressed from a recombinant plasmid could restore the ability to grow on medium without arginine. Moreover, cell extracts show a specific ASL activity of 16.2 nmoles of urea · min−1· (mg protein)−1. Partially purified, His-tagged ASL runs as a 53-kDa protein band in SDS-PAGE and about 215-kDa protein in native-PAGE, suggesting that the native protein is a tetramer.

Copyright information

© Springer-Verlag New York Inc. 2001

Authors and Affiliations

  • Olga Troshina
    • 1
  • Alfred Hansel
    • 1
  • Peter Lindblad
    • 1
  1. 1.Department of Physiological Botany, EBC, Uppsala University, Villavägen 6, SE-752 36 Uppsala, SwedenSE
  2. 2.Institute of Basic Biological Problems, Russian Academy of Sciences, Pushchino, Moscow Region, 142 290, RussiaRU
  3. 3.Molecular and Cellular Biophysics Research Unit, Medical Faculty of the Friedrich-Schiller University, Drackendorfer Strasse 1, D-07747 Jena, GermanyDE