Functional studies of Plasmodium falciparum's prohibitin1 and prohibitin 2 in yeast

Indian J Med Microbiol. 2020 Apr-Jun;38(2):213-215. doi: 10.4103/ijmm.IJMM_20_28.

Abstract

Prohibitins (PHBs) are evolutionarily conserved mitochondrial integral membrane proteins, shown to regulate mitochondrial structure and function, and can be classified into PHB1 and PHB2. PHB1 and PHB2 have been shown to interact with each other, and form heterodimers in mitochondrial inner membrane. Plasmodium falciparum has orthologues of PHB1 and PHB2 in its genome, and their role is unclear. Here, by homology modelling and yeast two-hybrid analysis, we show that putative Plasmodium PHBs (Pf PHB1 and Pf PHB2) interact with each other, which suggests that they could form supercomplexes of heterodimers in Plasmodium, the functional form required for optimum mitochondrial function.

Keywords: Mitochondria; Plasmodium falciparum; prohibitins; supercomplex; yeast two-hybrid analysis.

MeSH terms

  • Membrane Proteins / chemistry*
  • Mitochondria / metabolism
  • Models, Molecular
  • Plasmodium falciparum / chemistry*
  • Plasmodium falciparum / genetics
  • Prohibitins
  • Protein Conformation
  • Protein Multimerization
  • Protozoan Proteins / chemistry*
  • Repressor Proteins / chemistry*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins
  • Two-Hybrid System Techniques

Substances

  • Membrane Proteins
  • PHB1 protein, S cerevisiae
  • Prohibitins
  • Protozoan Proteins
  • Repressor Proteins
  • Saccharomyces cerevisiae Proteins