Characterization of DsrD and its interaction with the DsrAB dissimilatory sulfite reductase

Protein Sci. 2024 Dec;33(12):e5222. doi: 10.1002/pro.5222.

Abstract

Microbial dissimilatory sulfate reduction is a key process in the global sulfur and carbon cycles in anoxic ecosystems. In this anaerobic respiration, sulfate is phosphorylated and reduced to sulfite, which is further reduced to a DsrC-trisulfide by the dissimilatory sulfite reductase DsrAB. DsrD is a small protein that acts as an allosteric activator of DsrAB, increasing the efficiency of sulfite reduction. Here, we report a detailed study of DsrD and its interaction with DsrAB. Sequence similarity analyses show that there are three groups of DsrD in organisms with a reductive-type DsrAB. The protein regions involved in the DsrD-DsrAB interaction and activity-promoting effect were investigated through in vitro and in silico studies, including mutations of conserved DsrD residues. The results reveal that the conserved β-loop of DsrD is involved in the interaction, contributing to a better understanding of its mechanism of action.

Keywords: DsrAB; DsrD; dissimilatory sulfite reductase; sulfate‐reducing bacteria; sulfur metabolism.

MeSH terms

  • Bacterial Proteins* / chemistry
  • Bacterial Proteins* / genetics
  • Bacterial Proteins* / metabolism
  • Hydrogensulfite Reductase / chemistry
  • Hydrogensulfite Reductase / genetics
  • Hydrogensulfite Reductase / metabolism
  • Models, Molecular
  • Protein Binding
  • Sulfites / chemistry
  • Sulfites / metabolism

Substances

  • Bacterial Proteins
  • Hydrogensulfite Reductase
  • Sulfites