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YHS-domains are small protein modules which have been proposed to bind transition-metal ions like the related TRASH-domains. They are found in a variety of enzymes including copper-transporting ATPases and adenylyl cyclases. Here we investigate a class IIIc adenylyl cyclase from  Mycobacterium phlei  which contains a C-terminal YHS-domain linked to the catalytic domain by a peptide of 8 amino acids. We expressed the isolated catalytic domain and the full-length enzyme in  E .  coli . The catalytic domain requires millimolar Mn 2+  as a cofactor for efficient production of cAMP, is unaffected by low micromolar concentrations of Cu 2+  and inhibited by concentrations higher than 10 μM. The full-length enzyme also requires Mn 2+  in the absence of an activator. However, 1–10 μM Cu 2+  stimulate the  M .  phlei  adenylyl cyclase sixfold when assayed with Mn 2+ . With Mg 2+  as the probable physiological cofactor of the adenylyl cyclase Cu 2+  specifically switches the enzyme from an inactive to an active state. Other transition-metal ions do not elicit activity with Mg 2+ . We favor the view that the YHS-domain of  M .  phlei  adenylyl cyclase acts as a sensor for copper ions and signals elevated levels of the transition-metal via cAMP. By analogy to TRASH-domains binding of Cu 2+  probably occurs via one conserved aspartate and three conserved cysteine-residues in the YHS-domain.

The YHS-Domain of an Adenylyl Cyclase from Mycobacterium phlei Is a Probable Copper-Sensor Module