Kilbournase, a protease-associated domain subtilase secreted by the fungal corn pathogen Stenocarpella maydis

Todd A. Naumann, Michael J. Naldrett, Neil P.J. Price

Research output: Contribution to journalArticle

Abstract

Subtilases are a large family of serine proteases that occur throughout biology. A small subset contain protease-associated (PA) domains that are structurally separate from but encoded within the active site. In bacteria, subtilase PA domains function to recruit specific protein substrates. Here we demonstrate that a protease secreted by the fungal corn pathogen Stenocarpella maydis, which truncates corn ChitA chitinase, is a PA domain subtilase. Protease was purified from S. maydis cultures and tryptic peptides were analyzed by LC-MS/MS. Ions were mapped to two predicted PA domain subtilases. Yeast strains were engineered to express each protease. One failed to produce recombinant protein while the other secreted protease that truncated ChitA. This protease, that we named kilbournase, was purified and characterized. It cleaved multiple peptide bonds in the amino-terminal chitin binding domain of ChitA while leaving the catalytic domain intact. Kilbournase was more active on the ChitA-B73 alloform compared to ChitA-LH82 and did not cleave AtChitIV3, a homolog from Arabidopsis thaliana, indicating a high level of specificity. Truncation of corn ChitA by kilbournase resembles truncation of human C5a by Streptococcus pyogenes ScpA, arguing that PA domain proteases in bacteria and fungi may commonly target specific host proteins.

Original languageEnglish (US)
Article number103399
JournalFungal Genetics and Biology
Volume141
DOIs
StatePublished - Aug 2020

Keywords

  • Chitinases
  • Fungi
  • Recombinant proteins
  • Serine proteases
  • Substrate specificity
  • Zea mays

ASJC Scopus subject areas

  • Microbiology
  • Genetics

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