New perspectives of zinc coordination environments in proteins

Maret, Wolfgang

doi:10.1016/j.jinorgbio.2011.11.018

Cited by 159 publications

(114 citation statements)

References 81 publications

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“…4C). Cysteine, aspartate, and histidine residues are the most common sites for zinc coordination in proteins (37). To further confirm the coordination role of these three residues, we also conducted zinc titration with 13 C, 1 H-HSQC.…”

Section: Zinc Inhibits Hh Autoprocessingmentioning

confidence: 99%

Zinc Inhibits Hedgehog Autoprocessing

Xie

Owen

Xia³

et al. 2015

Journal of Biological Chemistry

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Background: In many types of cancers zinc deficiency and overproduction of Hedgehog (Hh) ligand co-exist. Results: Zinc binds to the active site of the Hedgehog-intein (Hint) domain and inhibits Hh ligand production both in vitro and in cell culture. Conclusion: Zinc influences the Hh autoprocessing.Significance: This study uncovers a novel mechanistic link between zinc and the Hh signaling pathway.

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Section: Zinc Inhibits Hh Autoprocessingmentioning

confidence: 99%

Zinc Inhibits Hedgehog Autoprocessing

Xie

Owen

Xia³

et al. 2015

Journal of Biological Chemistry

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“…Z inc-finger proteins (ZFs) are a large class of proteins that use zinc as structural cofactors (1)(2)(3)(4). ZFs perform a variety of functions ranging from the modulation of gene expression through specific interactions with DNA or RNA to the control of signaling pathways via protein-protein interactions.…”

mentioning

confidence: 99%

“…The general feature that defines a ZF protein is the presence of one or more domains that contain a combination of four cysteine and/or histidine residues that serve as ligands for zinc. When zinc binds to these ligands, the domain adopts the structure necessary for function (1)(2)(3)(4).…”

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confidence: 99%

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Cleavage and polyadenylation specificity factor 30: An RNA-binding zinc-finger protein with an unexpected 2Fe–2S cluster

Shimberg

Michalek

Oluyadi

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Cleavage and polyadenylation specificity factor 30 (CPSF30) is a key protein involved in pre-mRNA processing. CPSF30 contains five Cys 3 His domains (annotated as "zinc-finger" domains). Using inductively coupled plasma mass spectrometry, X-ray absorption spectroscopy, and UV-visible spectroscopy, we report that CPSF30 is isolated with iron, in addition to zinc. Iron is present in CPSF30 as a 2Fe-2S cluster and uses one of the Cys 3 His domains; 2Fe-2S clusters with a Cys 3 His ligand set are rare and notably have also been identified in MitoNEET, a protein that was also annotated as a zinc finger. These findings support a role for iron in some zinc-finger proteins. Using electrophoretic mobility shift assays and fluorescence anisotropy, we report that CPSF30 selectively recognizes the AU-rich hexamer (AAUAAA) sequence present in pre-mRNA, providing the first molecular-based evidence to our knowledge for CPSF30/RNA binding. Removal of zinc, or both zinc and iron, abrogates binding, whereas removal of just iron significantly lessens binding. From these data we propose a model for RNA recognition that involves a metaldependent cooperative binding mechanism.zinc | iron-sulfur | RNA | protein | binding

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“…These residues also coordinate Zn 2ϩ in high affinity binding sites of numerous proteins (22,23). Thus, pH changes may affect the interaction of Zn 2ϩ with its binding sites.…”

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confidence: 99%