Phylogenetic analysis of heavy-metal ATPases in fungi and characterization of the copper-transporting ATPase of Cochliobolus heterostrophus

Mycol Res. 2009 Jun-Jul;113(Pt 6-7):737-45. doi: 10.1016/j.mycres.2009.02.009. Epub 2009 Feb 26.

Abstract

We performed a phylogenetic analysis of heavy-metal ATPases (HMAs) in fungi and found that HMAs can be divided into three groups, A, B, and C. Group A is predicted to deliver copper ions to copper-containing proteins, while Groups B and C are thought to function as cell-membrane copper-efflux pumps. Furthermore, Groups B and C consist of fungal-specific HMAs, while Group A consists of fungal orthologues that have been well conserved in eukaryotes. We also cloned and characterized a Group A-type HMA gene (i.e., ChCcc2) of the filamentous plant pathogen, Cochliobolus heterostrophus. Mutation of ChCcc2 severely affected growth, pigmentation, conidiation, and colonial morphology. Activity of the copper-containing protein, laccase, was also lost in ChCcc2 mutants, suggesting that ChCCC2 plays an important role in growth and morphology by activating various copper-containing proteins in C. heterostrophus.

MeSH terms

  • Cation Transport Proteins / chemistry
  • Cation Transport Proteins / genetics
  • Cation Transport Proteins / metabolism*
  • Cloning, Molecular
  • Copper / metabolism
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics*
  • Fungal Proteins / metabolism
  • Fungi / chemistry
  • Fungi / classification
  • Fungi / enzymology*
  • Fungi / genetics*
  • Metals, Heavy / metabolism*
  • Mutation
  • Phylogeny*
  • Plant Diseases / microbiology
  • Protein Structure, Tertiary

Substances

  • Cation Transport Proteins
  • Fungal Proteins
  • Metals, Heavy
  • Copper