Inducible protein stabilization system in Leishmania mexicana

Lucie Podešvová, Huan Huang, Vyacheslav Yurchenko

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Targeted regulation of protein levels is an important tool to investigate the role of proteins essential for cell function and development. In recent years, methods based on the Escherichia coli dihydrofolate reductase destabilization domain (ecDHFR DD) have been established and used in various cell types. ecDHFR DD destabilizes the fused protein of interest and causes its degradation by proteasomes, unless it is stabilized by a specific ligand, trimethoprim. In this work we developed an inducible protein stabilization system in Leishmania mexicana based on ecDHFR DD.

Original languageEnglish (US)
Pages (from-to)62-64
Number of pages3
JournalMolecular and Biochemical Parasitology
Volume214
DOIs
StatePublished - Jun 1 2017

Fingerprint

Leishmania mexicana
Tetrahydrofolate Dehydrogenase
Escherichia coli
Proteins
Trimethoprim
Proteasome Endopeptidase Complex
Ligands

Keywords

  • ecDHFR
  • Leishmania mexicana
  • Protein stabilization
  • Trimethoprim

ASJC Scopus subject areas

  • Parasitology
  • Molecular Biology

Cite this

Inducible protein stabilization system in Leishmania mexicana. / Podešvová, Lucie; Huang, Huan; Yurchenko, Vyacheslav.

In: Molecular and Biochemical Parasitology, Vol. 214, 01.06.2017, p. 62-64.

Research output: Contribution to journalArticle

Podešvová, Lucie ; Huang, Huan ; Yurchenko, Vyacheslav. / Inducible protein stabilization system in Leishmania mexicana. In: Molecular and Biochemical Parasitology. 2017 ; Vol. 214. pp. 62-64.
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