S-Adenosylmethionine-Dependent Methyltransferase Helps Pichia caribbica Degrade Patulin

J Agric Food Chem. 2019 Oct 23;67(42):11758-11768. doi: 10.1021/acs.jafc.9b05144. Epub 2019 Oct 14.

Abstract

Patulin contamination not only is a menace to human health but also causes serious environmental problems worldwide due to the synthetic fungicides that are used to control it. This study focused on investigating the patulin degradation mechanism in Pichia caribbica at the molecular level. According to the results, P. caribbica (2 × 106 cells/mL) was able to degrade patulin from 20 μg/mL to an undetectable level in 72 h. The RNA-seq data showed patulin-induced oxidative stress and responses in P. caribbica. The deletion of PcCRG1 led to a significant decrease in patulin degradation by P. caribbica, whereas the overexpression of PcCRG1 accelerated the degradation of patulin. The study identified that PcCRG1 protein had the ability to degrade patulin in vitro. Overall, we demonstrated that the patulin degradation process in P. caribbica was more than one way; PcCRG1 was an S-adenosylmethionine-dependent methyltransferase and played an important role in the patulin degradation process in P. caribbica.

Keywords: PcCRG1; Pichia caribbica; biocontrol; degradation; patulin.

MeSH terms

  • Amino Acid Sequence
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Fungicides, Industrial / metabolism*
  • Methyltransferases / chemistry
  • Methyltransferases / genetics
  • Methyltransferases / metabolism*
  • Patulin / metabolism*
  • Pichia / enzymology
  • Pichia / genetics
  • Pichia / metabolism*
  • S-Adenosylmethionine / metabolism*
  • Sequence Alignment

Substances

  • Fungal Proteins
  • Fungicides, Industrial
  • S-Adenosylmethionine
  • Patulin
  • Methyltransferases