Understanding how cells allocate metals using metal sensors and metallochaperones.
Each metalloprotein must somehow acquire the correct metal. We review the insights into metal specificity in cells provided by studies of ArsR-SmtB DNA binding, metal-responsive transcriptional repressors, and a bacterial copper chaperone. Cyanobacteria are the one bacterial group that have known enzymatic demand for cytoplasmic copper import. The copper chaperone and ATPases that supply cyanobacterial plastocyanin and cytochrome oxidase are reviewed, along with related ATPases for cobalt and zinc. These studies highlight the contributions of protein-protein interactions to metal speciation. Metal sensors and metallochaperones, along with metal transporters and metal-storage proteins, act in concert not only to supply the correct metals but also to withhold the wrong ones.
Tottey
Stephen
S
Institute for Cell and Molecular Biosciences, Medical School, University of Newcastle, NE2 4HH, United Kingdom.
Harvie
Duncan R
DR
Robinson
Nigel J
NJ
D001692:Biological Transport; D003035:Cobalt / Q000378:metabolism; D003300:Copper / Q000378:metabolism*; D000458:Cyanobacteria / Q000201:enzymology* / Q000378:metabolism; D008667:Metalloproteins / Q000378:metabolism*; D008958:Models, Molecular; D015032:Zinc / Q000378:metabolism
D008667:Metalloproteins; D003035:Cobalt; D003300:Copper; D015032:Zinc