Abstract
Zinc (Zn) is the quintessential d block metal, needed for survival in all living organisms. While Zn is an essential element, its excess is deleterious, therefore, maintenance of its intracellular concentrations is needed for survival. The living organisms, during the course of evolution, developed proteins that can track the limitation or excess of necessary metal ions, thus providing survival benefits under variable environmental conditions. Zinc uptake regulator (Zur) is a regulatory transcriptional factor of the FUR superfamily of proteins, abundant among the bacterial species and known for its intracellular Zn sensing ability. In this study, we highlight the roles played by Zur in maintaining the Zn levels in various bacterial species as well as the fact that in recent years Zur has emerged not only as a Zn homeostatic regulator but also as a protein involved directly or indirectly in virulence of some pathogens. This functional aspect of Zur could be exploited in the ventures for the identification of newer antimicrobial targets. Despite extensive research on Zur, the insights into its overall regulon and its moonlighting functions in various pathogens yet remain to be explored. Here in this review, we aim to summarise the disparate functional aspects of Zur proteins present in various bacterial species.
Highlights
Background of Zinc uptake regulator (Zur)Zur (Zinc Uptake Regulator) is a Zn-sensing transcriptional regulator that is a member of the FUR superfamily of metal-sensing transcriptional regulators
While uptake of Zn is regulated by proteins such as zinc uptake regulator, known as Zur (Fur family transcriptional regulator) or AdcR (MarR/SlyA family), the export/sequestration is regulated by proteins like ZntR or members of ArsR/SmtB
Zur was initially identified in E. coli [71] as a pivotal protein for Zn homeostasis and further in other organisms including B. subtilis [72,73,74], L. monocytogenes [75], Xanthomonas campestris [76], S. coelicolor [17], Streptococcus sp. [77], Enterococcus faecalis [78] and Mycobacterium tuberculosis [79]
Summary
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. It binds to certain proteins which play a key role in gene expression such as ribosomal proteins, RNA polymerases, tRNA synthetases, certain specific transcription factors and sigma factor interacting proteins [3]. It averts the free radical formation and works as an antioxidant protecting the sulfhydryl groups from the free radical attack. It has a strong ability to bind proteins in comparison to other divalent metals, its excess intracellular concentrations can give rise to pleiotropic effects in the cellular proteome due to mismetallation, causing alterations in the expression or activity of Zn containing proteins [13]. The varied roles played by Zn within the organism highlight the importance of its homeostasis for survival
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