Open AccessGlutathione transferase‐like proteins encoded in genomes of yeasts and fungi: insights into evolution of a multifunctional protein superfamily
Author(s) -
McGoldrick Shane,
O'Sullivan Siobhàn M.,
Sheehan David
Publication year - 2005
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/j.femsle.2004.10.033
Subject(s) - biology , genetics , gene , fungal protein , genome , sequence alignment , sequence analysis , peptide sequence , computational biology , protein domain
Most fungal glutathione transferases (GSTs) do not fit easily into any of the previously characterised classes by immunological, sequence or catalytic criteria. In contrast to the paucity of studies on GSTs cloned or isolated from fungal sources, a screen of databases revealed 67 GST‐like sequences from 21 fungal species. Comparison by multiple sequence alignment generated a dendrogram revealing five clusters of GST‐like proteins designated clusters 1, 2, EFIBγ, Ure2p and MAK16, the last three of which have previously been related to the GST superfamily. Surprisingly, a relatively small number of fungal GSTs belong to mainstream classes and the previously‐described fungal Gamma class is not widespread in the 21 species studied. Representative crystal structures are available for the EFIBγ and Ure2p classes and the domain structures of representative sequences are compared with these. In addition, there are some “orphan” sequences that do not fit into any previously‐described class, but show similarity to genes implicated in fungal biosynthetic gene clusters. We suggest that GST‐like sequences are widespread in fungi, participating in a wide range of functions. They probably evolved by a process similar to domain “shuffling”.