Phylogenetic analysis of heavy-metal ATPases in fungi and characterization of the copper-transporting ATPase of Cochliobolus heterostrophus.
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.
Saitoh
Yoshimoto
Y
Laboratory of Environmental Mycoscience, Graduate School of Agriculture, Kyoto University, Kitashirakawa oiwakecho 1, Sakyo-ku, Kyoto 606-8502, Japan.
Izumitsu
Kosuke
K
Tanaka
Chihiro
C
D027682:Cation Transport Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D003300:Copper / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D005658:Fungi / Q000737:chemistry / Q000145:classification / Q000201:enzymology* / Q000235:genetics*; D019216:Metals, Heavy / Q000378:metabolism*; D009154:Mutation; D010802:Phylogeny; D010935:Plant Diseases / Q000382:microbiology; D017434:Protein Structure, Tertiary
D027682:Cation Transport Proteins; D005656:Fungal Proteins; D019216:Metals, Heavy; D003300:Copper