Cysteine and histidine shuffling: mixing and matching cysteine and histidine residues in zinc finger proteins to afford different folds and function

Michalek, Jamie L.; Besold, Angelique N.; Michel, Sarah L. J.

doi:10.1039/c1dt11071c

Cited by 52 publications

(114 citation statements)

References 197 publications

Supporting

Mentioning

113

Contrasting

Unclassified

Order By: Relevance

“…1). As a class, these proteins are predicted to be involved in RNA regulation; however, the function(s) of most of these proteins have not yet been established (1,2,10,11).…”

mentioning

confidence: 99%

“…This class is composed of ZFs that contain a Cys 2 His 2 domain (CysX 2-5 CysX 12-13 HisX 3-5 His). Classical ZFs adopt an alphahelical/antiparallel beta-sheet structure when zinc is coordinated and bind DNA in a sequence-specific manner (2,4). The remaining classes of ZFs are collectively called "nonclassical" ZFs (1).…”

mentioning

confidence: 99%

“…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).…”

mentioning

confidence: 99%

“…One important Cys 3 His ZF protein is cleavage and polyadenylation specificity factor 30 (CPSF30) (2,12). CPSF30 contains five Cys 3 His domains.…”

mentioning

confidence: 99%

See 4 more Smart Citations

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.

Self Cite

View full text Add to dashboard Cite

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

show abstract

“…1). As a class, these proteins are predicted to be involved in RNA regulation; however, the function(s) of most of these proteins have not yet been established (1,2,10,11).…”

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

“…One important Cys 3 His ZF protein is cleavage and polyadenylation specificity factor 30 (CPSF30) (2,12). CPSF30 contains five Cys 3 His domains.…”

mentioning

confidence: 99%

See 3 more Smart Citations

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.

Self Cite

View full text Add to dashboard Cite

show abstract

Encyclopedia of Inorganic and Bioinorganic Chemistry

Giansiracusa

Gransbury²,

Chilton

et al. 2011

View full text Add to dashboard Cite

Single-Molecule Magnets (SMMs) are finite molecular species that display slow relaxation of their magnetisation, equivalent to a magnetic memory effect. Here we give an overview of how SMM behaviour can arise from the spin properties of a giant molecular spin or unpaired electrons on a single metal centre. We outline the criteria for obtaining SMM properties, and how these have developed through theoretical insight to lead to the rapid advancement of SMM performance. We discuss the progression of the field from the original Mn12 polymetallic cluster, to carefully engineered coordination complexes of Ln ions. Classes of compounds discussed include 3d, 3d-4f and 4f polymetallic clusters, 3d and 4f monometallic complexes, and homo-and hetero-metallic exchange-coupled SMMs, including those bridged by radical ligands and/or encapsulated in endohedral fullerenes. The state-ofthe-art in SMMs is discussed, leaving the reader with an up-to-date understanding of theory and synthetic design, with references to comprehensive reviews.For readers new or returning to the area, we highlight the standard experiments used to characterise SMMs -including magnetic hysteresis, zero-field cooled/field cooled magnetic susceptibility, alternating current susceptibility and magnetisation decay measurements. We highlight the common pitfalls often encountered in the literature in measurements, data analysis and structural correlation of properties. We aim to provide a clear background for relaxation mechanisms in SMMs and the quantification of performance using energy barriers, blocking temperatures and relaxation rate. The reader is directed towards a series of proof-ofconcept publications which have spearheaded the implementation of SMMs towards future applications in high density data storage, quantum information processing and spintronics.

show abstract

The Interaction of Metal Compounds with Protein Targets: New Tools in Medicinal Chemistry and Chemical Biology

Miller

Gomes

Storr

et al. 2017

Encyclopedia of Inorganic and Bioinorganic Chemistry

View full text Add to dashboard Cite

In cells and organisms, metal complexes can be specifically designed to interact with biomolecules and accordingly alter important biological processes. These interactions have been widely explored for targeting specific biological functions and diseases. In fact, several studies have demonstrated that inorganic chemistry offers significant diversity and versatility for the preparation of highly potent protein modulators (e.g., inhibitors). Moreover, both coordination and organometallic complexes featuring favorable chemico‐physical properties (e.g., luminescence) have proven to be well suited to image proteins and peptides in living cells by various methods. An inherent advantage of metal complexes is the accessibility of multiple oxidation states, and overall charge and geometries, which makes them attractive from the point of view of chemical design. However, these properties can become a disadvantage if not controlled and fine‐tuned in the biological application. In this review, we generally discuss the use of metal compounds, targeting proteins and/or peptides, in medicinal chemistry and chemical biology, and then focus on representative recent examples and applications. Furthermore, we highlight future challenges and attractive perspectives in the field, which may stimulate research and define new frontiers in bioinorganic chemistry.

show abstract

Cysteine and histidine shuffling: mixing and matching cysteine and histidine residues in zinc finger proteins to afford different folds and function

Cited by 52 publications

References 197 publications

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

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

Encyclopedia of Inorganic and Bioinorganic Chemistry

The Interaction of Metal Compounds with Protein Targets: New Tools in Medicinal Chemistry and Chemical Biology

Contact Info

Product

Resources

About