التفاصيل البيبلوغرافية
العنوان: |
Zng1 is a GTP-dependent zinc transferase needed for activation of methionine aminopeptidase |
المؤلفون: |
Miriam Pasquini, Nicolas Grosjean, Kim K. Hixson, Carrie D. Nicora, Estella F. Yee, Mary Lipton, Ian K. Blaby, John D. Haley, Crysten E. Blaby-Haas |
المصدر: |
Cell Reports, Vol 39, Iss 7, Pp 110834- (2022) |
بيانات النشر: |
Elsevier, 2022. |
سنة النشر: |
2022 |
المجموعة: |
LCC:Biology (General) |
مصطلحات موضوعية: |
MetAP, insertase, NME, GTPase, zinc homeostasis, nutrient limitation, Biology (General), QH301-705.5 |
الوصف: |
Summary: 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. |
نوع الوثيقة: |
article |
وصف الملف: |
electronic resource |
اللغة: |
English |
تدمد: |
2211-1247 |
Relation: |
http://www.sciencedirect.com/science/article/pii/S2211124722006076; https://doaj.org/toc/2211-1247 |
DOI: |
10.1016/j.celrep.2022.110834 |
URL الوصول: |
https://doaj.org/article/811d242cdd1a4388bf0c863ee91ee07a |
رقم الانضمام: |
edsdoj.811d242cdd1a4388bf0c863ee91ee07a |
قاعدة البيانات: |
Directory of Open Access Journals |