3 Chemical Properties of Zn2+ for the Zn-Proteome. 1 ... This article was published in the Encyclopedia of Inorganic and Bioinorganic Chemistry in 2015 by John ...
Zinc Proteomics
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Andrew Nowakowski1 , Mohammad Karim2 & David Petering2
The word ‘‘proteomics’’ connotes the methods developed and the knowledge discovered during the study of large numbers of proteins in aggregate. The term ‘‘Zn-proteomics’’ is useful when it stimulates novel research questions. For instance, what are the properties of Zn2+ that render it widely useful as a functional and structural cofactor within the Znproteome? What are the mechanisms of Zn2+ trafficking from extracellular media into the cellular Zn-proteome? How does Zn2+ traffic between specific proteins during signaling? What research tools are available to address such questions? This review addresses these questions in mammalian systems.
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Northwestern University, Evanston, IL, USA University of Wisconsin-Milwaukee, Milwaukee, WI, USA
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Introduction: The Zinc-Proteome, A Global View Meaning and Utility of the Term ‘‘Zn Proteomics’’ Chemical Properties of Zn2+ for the Zn-Proteome Trafficking of Extracellular Zn2+ to apo-Zn-Proteins Involvement of Metallothionein in Zn2+ Trafficking Zinc Sensing and Signaling: Proteomic Considerations Physiological and Pathological Modifications of the Zn-Proteome Tools for Studying the Zn-Proteome Conclusion Acknowledgments References Further Reading
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MEANING AND UTILITY OF THE TERM ‘‘Zn PROTEOMICS’’
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INTRODUCTION: THE ZINC-PROTEOME, A GLOBAL VIEW
Life is hierarchically organized.1 Cellular life provides the foundation for increasingly complex systems of organisms, ecosystems, and the biosphere. Systems biology seeks to understand how the members of each level function and interact to generate holistic behavior.2,3 Initially, scientists turned to sequencing the genome and describing global gene expression.3 Coupled with the knowledge of molecular biology, genomic information provides estimates of the numbers of proteins that can be expressed in cells, their amino acid sequences, and information about coordinated regulation of their expression.4 However, the sheer quantity of such information focuses researchers pragmatically on tractable subsets of proteins of functional significance within particular cells and organisms. A substantial fraction of the proteome binds metal ions. Bioinformatic analyses estimate that mammals express about 3000 Zn-proteins that together constitute their Zn-proteome.5,6 Remarkably, this analysis suggests that 9–10% of cellular proteins require Zn2+ , far more than those utilizing nonheme iron (1%) or Cu (
