Abstract
The DING proteins are ubiquitous in the three domains of life, from mesophiles to thermo- and hyperthermophiles. They belong to a family of more than sixty members and have a characteristic N-terminus, DINGGG, which is considered a “signature” of these proteins. Structurally, they share a highly conserved phosphate binding site, and a three dimensional organization resembling the “Venus Flytrap”, both reminding the ones of PstS proteins. They have unusually high sequence conservation, even between distantly related species. Nevertheless despite that the genomes of most of these species have been sequenced, the DING gene has not been reported for all the relative characterized DING proteins. Identity of known DING proteins has been confirmed immunologically and, in some cases, by N-terminal sequence analysis. Only a few of the DING proteins have been purified and biochemically characterized. DING proteins are heterogeneous for their wide range of biological activities and some show different activities not always correlated with each other. Most of them have been originally identified for different biological properties, or rather for binding to phosphate and also to other ligands. Their involvement in pathologies is described. This review is an update of the most recent findings on old and new DING proteins.
Highlights
Considering almost 600 proposed inteins have been described, spanning all three domains of life [63], it is intriguing to think that a “protein splicing-like” mechanism for DING proteins may exist in some bacteria and Archaea.This aspect could be more deeply investigated to try to clarify this “apparent” lack of the DING genes
The world of DING proteins is very complex and they represent more than merely components of a membrane phosphate transport system [2]
The activation of bacterial alkaline phosphatase biosynthesis upon phosphate starvation is a classic example of induced enzyme biosynthesis in bacteria [64], which involves transmembrane signaling regulated by the level of phosphate in the environment
Summary
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. In the same year Sachdeva et al (2013) [3] published a paper comparing the amino acid sequences of the most studied mesophilic DINGs from both prokaryotes and eukaryotes, highlighting both their common primary structure and basic similarity with PstS and alkaline phosphatase configuration (Venus flytrap model). This extends the structural features in common with different DING proteins. In line with the above overview of main features of DING proteins, we will present the state of the art of the DING proteins identified in Prokaryotes, Eukarya and extremophilic environment
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