| First Author | Pasquini M | Year | 2022 |
| Journal | Cell Rep | Volume | 39 |
| Issue | 7 | Pages | 110834 |
| PubMed ID | 35584675 | Mgi Jnum | J:326189 |
| Mgi Id | MGI:7294463 | Doi | 10.1016/j.celrep.2022.110834 |
| Citation | Pasquini M, et al. (2022) Zng1 is a GTP-dependent zinc transferase needed for activation of methionine aminopeptidase. Cell Rep 39(7):110834 |
| abstractText | The evolution of zinc (Zn) as a protein cofactor altered the functional landscape of biology, but dependency on Zn also created an Achilles' heel, necessitating adaptive mechanisms to ensure Zn availability to proteins. A debated strategy is whether metallochaperones exist to prioritize essential Zn-dependent proteins. Here, we present evidence for a conserved family of putative metal transferases in human and fungi, which interact with Zn-dependent methionine aminopeptidase type I (MetAP1/Map1p/Fma1). Deletion of the putative metal transferase in Saccharomyces cerevisiae (ZNG1; formerly YNR029c) leads to defective Map1p function and a Zn-deficiency growth defect. In vitro, Zng1p can transfer Zn(2+) or Co(2+) to apo-Map1p, but unlike characterized copper chaperones, transfer is dependent on GTP hydrolysis. Proteomics reveal mis-regulation of the Zap1p transcription factor regulon because of loss of ZNG1 and Map1p activity, suggesting that Zng1p is required to avoid a compounding effect of Map1p dysfunction on survival during Zn limitation. |
