Production of soluble, active acetyl serotonin methyl transferase in Leishmania tarentolae

Mariem Ben-Abdallah (1) , Vincent Bondet (1) , Fabien Fauchereau (2) , Pierre Béguin (1) , Hany Goubran-Botros (1) , Cécile Pagan (1) , Thomas Bourgeron (2) , Jacques Bellalou (1)

1 Production de Protéines Recombinantes et d'Anticorps (Plate-Forme)
2 Génétique Humaine et Fonctions Cognitives

N-acetyl serotonin methyl transferase (ASMT) is the last enzyme in the melatonin synthesis pathway. Evidence linking autism-related disorders with disorders of melatonin metabolism, and, more specifically, with mutations of the gene encoding ASMT, prompted us to investigate the properties and localization of this enzyme. As a first step, we undertook to overproduce the protein in a recombinant host. Early attempts to produce ASMT in recombinant Escherichia coli yielded only insoluble and heavily degraded material. However, recombinant ASMT (rASMT) could be produced in soluble, active form and purified in milligram amounts when the gene was cloned and expressed in Leishmania tarentolae.

Domains: Life Sciences [q-bio]

Mariem Ben-Abdallah, Vincent Bondet, Fabien Fauchereau, Pierre Béguin, Hany Goubran-Botros, et al.. Production of soluble, active acetyl serotonin methyl transferase in Leishmania tarentolae. Protein Expression and Purification, 2011, 75 (1), pp.114-118. ⟨10.1016/j.pep.2010.07.011⟩. ⟨pasteur-03251902⟩