The unique fold and lability of the [2Fe‑2S] clusters of NEET proteins mediate their key functions in health and disease

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This article discusses the NEET fold and its structural elements.

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14 p.

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Karmi, Ola; Marjault, Henri-Baptiste; Pesce, Luca; Carloni, Paolo; Onuchic, José N.; Jennings, Patricia A. et al. February 12, 2018.

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This article discusses the NEET fold and its structural elements.

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14 p.

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Abstract: NEET proteins comprise a new class of [2Fe-2S] cluster proteins. In human, three genes encode for NEET proteins: cisd1 encodes mitoNEET (mNT), cisd2 encodes the Nutrient-deprivation autophagy factor-1 (NAF-1) and cisd3 encodes MiNT (Miner2). These recently discovered proteins play key roles in many processes related to normal metabolism and disease. Indeed, NEET proteins are involved in iron, Fe-S, and reactive oxygen homeostasis in cells and play an important role in regulating apoptosis and autophagy. mNT and NAF-1 are homodimeric and reside on the outer mitochondrial membrane. NAF-1 also resides in the membranes of the ER associated mitochondrial membranes (MAM) and the ER. MiNT is a monomer with distinct asymmetry in the molecular surfaces surrounding the clusters. Unlike its paralogs mNT and NAF-1, it resides within the mitochondria. NAF-1 and mNT share similar backbone folds to the plant homodimeric NEET protein (At-NEET), while MiNT’s backbone fold resembles a bacterial MiNT protein. Despite the variation of amino acid composition among these proteins, all NEET proteins retained their unique CDGSH domain harboring their unique 3Cys:1His [2Fe-2S] cluster coordination through evolution. The coordinating exposed His was shown to convey the lability to the NEET proteins’ [2Fe-2S] clusters. In this minireview, we discuss the NEET fold and its structural elements. Special attention is given to the unique lability of the NEETs’ [2Fe-2S] cluster and the implication of the latter to the NEET proteins’ cellular and systemic function in health and disease.

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  • Journal of Biological Inorganic Chemistry, 2018. New York, NY: Springer

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  • Publication Title: Journal of Biological Inorganic Chemistry
  • Volume: 23
  • Pages: 599-612
  • Peer Reviewed: Yes

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UNT Scholarly Works

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  • February 12, 2018

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  • December 4, 2017

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  • January 26, 2018

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  • July 30, 2018, 12:01 p.m.

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Karmi, Ola; Marjault, Henri-Baptiste; Pesce, Luca; Carloni, Paolo; Onuchic, José N.; Jennings, Patricia A. et al. The unique fold and lability of the [2Fe‑2S] clusters of NEET proteins mediate their key functions in health and disease, article, February 12, 2018; New York, New York. (https://digital.library.unt.edu/ark:/67531/metadc1213691/: accessed June 19, 2019), University of North Texas Libraries, Digital Library, https://digital.library.unt.edu; crediting UNT College of Arts and Sciences.