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http://purl.uniprot.org/citations/35584675http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/35584675http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/35584675http://www.w3.org/2000/01/rdf-schema#comment"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 Zn2+ or Co2+ 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."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2022.110834"xsd:string
http://purl.uniprot.org/citations/35584675http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2022.110834"xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/author"Blaby I.K."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/author"Blaby I.K."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/author"Blaby-Haas C.E."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/author"Blaby-Haas C.E."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/author"Grosjean N."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/author"Grosjean N."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/author"Haley J.D."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/author"Haley J.D."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/author"Hixson K.K."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/author"Hixson K.K."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/author"Lipton M."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/author"Lipton M."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/author"Nicora C.D."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/author"Nicora C.D."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/author"Pasquini M."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/author"Pasquini M."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/author"Yee E.F."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/author"Yee E.F."xsd:string
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/35584675http://purl.uniprot.org/core/date"2022"xsd:gYear