Dimerization of long hibernation promoting factor from Staphylococcus aureus: Structural analysis and biochemical characterization

J Struct Biol. 2020 Jan 1;209(1):107408. doi: 10.1016/j.jsb.2019.107408. Epub 2019 Oct 25.

Abstract

Staphylococcus aureus hibernation promoting factor (SaHPF) is responsible for the formation of 100S ribosome dimers, which in turn help this pathogen to reduce energy spent under unfavorable conditions. Ribosome dimer formation strongly depends on the dimerization of the C-terminal domain of SaHPF (CTDSaHPF). In this study, we solved the crystal structure of CTDSaHPF at 1.6 Å resolution and obtained a precise arrangement of the dimer interface. Residues Phe160, Val162, Thr171, Ile173, Tyr175, Ile185 andThr187 in the dimer interface of SaHPF protein were mutated and the effects were analyzed for the formation of 100S disomes of ribosomes isolated from S. aureus. It was shown that substitution of any of single residues Phe160, Val162, Ile173, Tyr175 and Ile185 in the SaHPF homodimer interface abolished the ribosome dimerization in vitro.

Keywords: Hibernation; Long HPF; Ribosome; Staphylococcus aureus; X-ray.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / ultrastructure
  • Cryoelectron Microscopy
  • Dimerization
  • Hibernation / genetics
  • Humans
  • Protein Binding / genetics
  • Ribosomal Proteins / chemistry
  • Ribosomal Proteins / genetics*
  • Ribosomal Proteins / ultrastructure
  • Ribosomes / genetics*
  • Ribosomes / ultrastructure
  • Staphylococcal Infections / genetics*
  • Staphylococcal Infections / microbiology
  • Staphylococcus aureus / pathogenicity
  • Staphylococcus aureus / ultrastructure*

Substances

  • Bacterial Proteins
  • HPF protein, Staphylococcus aureus
  • Ribosomal Proteins