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Zinc and the Zinc Proteome

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Book cover Metallomics and the Cell

Part of the book series: Metal Ions in Life Sciences ((MILS,volume 12))

Abstract

Zinc(II) ions are catalytic, structural, and regulatory cofactors in proteins. In contrast to painstakingly collecting the pieces by isolating and characterizing zinc proteins, ‘omics’ approaches are now allowing us to tease out information about zinc proteins from genomes and to piece together the information to a broader knowledge and appreciation of the role of zinc in biology. Estimates for the number of zinc proteins in the human genome and in genomes of other organisms have been derived from a bioinformatics approach: mining sequence databases for homologies of known zinc-coordination motifs with characteristic ligand signatures for metal binding and combining this information with the knowledge about metal-binding domains of proteins. This approach resulted in an impressive number of almost 3000 human zinc proteins and made major contributions to our understanding of the composition of the zinc proteome and the functions of zinc proteins. However, the impact of zinc on protein science is even greater. Predictions do not include yet undiscovered ligand signatures, coordination environments that employ complex binding patterns with nonsequential binding of ligands and ligand bridges, zinc/protein interactions at protein interfaces, and transient interactions of zinc(II) ions with proteins that are not known to be zinc proteins. All this information and recent discoveries of how cellular zinc is controlled and how zinc(II) ions function as signaling ions add an hitherto unrecognized dimension to the zinc proteome of multicellular eukaryotic organisms. Zinc proteomics employs a combination of approaches from different disciplines, such as bioinformatics, biology, inorganic biochemistry, and significantly, analytical and structural chemistry. It provides crucial large-scale datasets for interpreting the roles of zinc in health and disease at both a molecular and a global, systems biology, level.

Please cite as: Met. Ions Life Sci. 12 (2013) 479–501

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Abbreviations

BMP:

bone morphogenetic protein

C:

cysteine

CERM:

Magnetic Resonance Center at the University of Florence

D:

aspartic acid

DALY:

disability-adjusted life years

E:

glutamic acid

EF-Ts:

elongation factor thermostable (translation elongation factor)

ER:

endoplasmic reticulum

H:

histidine

hK:

human kallikrein

IAPP:

islet amyloid polypeptide

IC50:

inhibition constant at 50% inhibition

LTA4:

leukotriene A4

MRE:

metal-response element

MT:

metallothionein

MTF-1:

metal-response element-binding transcription factor-1

NMDA:

N-methyl-d-aspartic acid

PCR:

polymerase chain reaction

PDB:

Protein Data Bank

PSA:

prostate-specific antigen

PTP:

protein tyrosine phosphatase

TFIIIA:

transcription factor IIIA

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Authors and Affiliations

  1. King’s College London, School of Medicine, Diabetes and Nutritional Sciences Division, Metal Metabolism Group, London, SE1 9NH, UK

    Wolfgang Maret

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  1. Centro Risonanze Magnetiche, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino, 50019, Firenze, Italy

    Lucia Banci

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Maret, W. (2013). Zinc and the Zinc Proteome. In: Banci, L. (eds) Metallomics and the Cell. Metal Ions in Life Sciences, vol 12. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-5561-1_14

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