MassIVE MSV000088135

Complete Public PXD028687

A conserved nucleotide-dependent metal chaperone for managing the cellular zinc economy during zinc limitation

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Description

How cells safeguard essential zinc-dependent functions during zinc deficiency is poorly understood. A long-debated strategy is whether soluble metal-trafficking chaperones exist to prioritize specific zinc-dependent proteins. We identified a eukaryotic family of metallochaperones that physically interacts with zinc-dependent methionine aminopeptidase type I (MAP1) in human and yeast. Deletion of the yeast metallochaperone-encoding gene NMC1 (formerly YNR029c) leads to a zinc-deficiency growth defect and defective initiator methionine cleavage caused by loss of Map1p activity. To better understand the observed fitness defects due to the lack of NMC1 under zinc deficiency, we used proteomics with Tandem Mass Tag (TMT) quantitation derived from WT, nmc1Delta, and map2Delta nmc1Delta strains grown in zinc-limited (1 uM) or zinc-replete (100 uM) conditions. Proteomics reveal global impacts due to the loss of NMC1 and Map1p function, including mis-regulation of the Zap1p regulon, and suggests that Nmc1p is required to avoid a compounding effect of Map1p dysfunction on cell survival during zinc deficiency. [doi:10.25345/C5CC2G] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: MetAP ; GTPase ; zinc starvation ; nutrient limitation

Contact

Principal Investigators:
(in alphabetical order) 		Crysten Blaby-Haas, Brookhaven National Laboratory, USA
Submitting User: alchemistmatt

Publications

Pasquini M, Grosjean N, Hixson KK, Nicora CD, Yee EF, Lipton M, Blaby IK, Haley JD, Blaby-Haas CE.
Zng1 is a GTP-dependent zinc transferase needed for activation of methionine aminopeptidase.
Cell Rep. 2022 May 17;39(7):110834.

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