Structural and functional relationships between type 1B heavy metal-transporting P-type ATPases in Arabidopsis.

Arabidopsis is remarkable for having eight members of the type 1B heavy metal-transporting P-type ATPase subfamily. Sequence analyses indicate that four, two of which may be targeted to plastids, are related to known Cu(I) transporters and contain N-terminal metal-binding site (MBS) motifs similar to those identified in other organisms. The remaining four are more closely related to known divalent cation transporters of prokaryotes. Three of these form a closely related group and are believed to be Zn(II) transporters. These contain a predicted N-terminal MBS that is a variant of those found in Cu transporters in addition to extended C-terminal regions that contain likely metal-binding sequences. Our current limited knowledge of the physiological roles of these transporters is reviewed and their evolutionary relationships are explored, including an hypothesis that some, particularly the putative divalent cation transporters, are derived from horizontal gene transfer events.