Ca2+-binding protein from Entamoeba histolytica (EhCaBP6) is a novel GTPase

Biochem Biophys Res Commun. 2020 Jun 30;527(3):631-637. doi: 10.1016/j.bbrc.2020.04.141. Epub 2020 May 16.

Abstract

GTPases are molecular switches, which regulate a variety of cellular processes such as cell polarity, gene transcription, microtubule dynamics, cell-cycle etc. In this paper, we characterize a Ca2+-binding protein from Entamoeba histolytica (EhCaBP6) as a novel GTPase. We locate the active site for GTP hydrolysis within the C-terminal domain of EhCaBP6, although it requires full length protein for its complete range of activity. Using NMR studies, we observe that GTP binding induces conformational change in EhCaBP6. The identification of this novel and unusual Ca2+-dependent GTPase is important to elucidate the unconventional cell cycle of E. histolytica.

Keywords: Ca(2+)-binding proteins; Entamoeba histolytica; GTPase; NMR Spectroscopy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calcium-Binding Proteins / chemistry
  • Calcium-Binding Proteins / metabolism*
  • Entamoeba histolytica / chemistry
  • Entamoeba histolytica / metabolism*
  • Entamoebiasis / parasitology
  • GTP Phosphohydrolases / chemistry
  • GTP Phosphohydrolases / metabolism*
  • Guanosine Triphosphate / metabolism
  • Humans
  • Molecular Docking Simulation
  • Protein Conformation
  • Protozoan Proteins / chemistry
  • Protozoan Proteins / metabolism*

Substances

  • Calcium-Binding Proteins
  • Protozoan Proteins
  • Guanosine Triphosphate
  • GTP Phosphohydrolases