Arginine methyltransferases PRMT2 and PRMT3 are essential for biosynthesis of plant-polysaccharide-degrading enzymes in Penicillium oxalicum

PLoS Genet. 2023 Jul 31;19(7):e1010867. doi: 10.1371/journal.pgen.1010867. eCollection 2023 Jul.

Abstract

Many filamentous fungi produce plant-polysaccharide-degrading enzymes (PPDE); however, the regulatory mechanism of this process is poorly understood. A Gal4-like transcription factor, CxrA, is essential for mycelial growth and PPDE production in Penicillium oxalicum. Its N-terminal region, CxrAΔ207-733 is required for the regulatory functions of whole CxrA, and contains a DNA-binding domain (CxrAΔ1-16&Δ59-733) and a methylated arginine (R) 94. Methylation of R94 is mediated by an arginine N-methyltransferase, PRMT2 and appears to induce dimerization of CxrAΔ1-60. Overexpression of prmt2 in P. oxalicum increases PPDE production by 41.4-95.1% during growth on Avicel, compared with the background strain Δku70;hphR+. Another arginine N-methyltransferase, PRMT3, appears to assist entry of CxrA into the nucleus, and interacts with CxrAΔ1-60 in vitro under Avicel induction. Deletion of prmt3 resulted in 67.0-149.7% enhanced PPDE production by P. oxalicum. These findings provide novel insights into the regulatory mechanism of fungal PPDE production.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arginine
  • Cellulose
  • Penicillium* / genetics
  • Protein-Arginine N-Methyltransferases* / genetics

Substances

  • PRMT2 protein, human
  • Protein-Arginine N-Methyltransferases
  • Cellulose
  • Arginine

Supplementary concepts

  • Penicillium oxalicum

Grants and funding

This work was financially supported by grant U21A20178 from the National Natural Science Foundation of China (to J.X.F.). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.