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Published on: December 17, 2013
DING Proteins Extend to the Extremophilic World
Elena Porzio1, Maria Rosaria Faraone Mennella2, Giuseppe Manco1
1Institute of Biochemistry and Cell Biology, CNR, Via P. Castellino 111, 80131 Naples, Italy.
DING proteins, found across all life domains, exhibit high sequence conservation and bind phosphate. This review updates recent findings on their diverse biological activities and roles in pathologies.
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Science
Background:
- DING proteins are a large, conserved protein family found in all domains of life.
- They possess a characteristic DINGGG N-terminus and a conserved phosphate-binding site, structurally similar to PstS proteins.
- Despite high sequence conservation, DING genes are not identified for all characterized DING proteins.
Purpose of the Study:
- To provide an updated review of recent findings on DING proteins.
- To highlight the diversity in biological activities and ligand-binding properties of DING proteins.
- To discuss the involvement of DING proteins in various pathologies.
Main Methods:
- Literature review of existing studies on DING proteins.
- Immunological and N-terminal sequence analysis for protein identity confirmation.
- Biochemical characterization of purified DING proteins.
Main Results:
- DING proteins are ubiquitous, with over sixty members identified across mesophilic, thermophilic, and hyperthermophilic organisms.
- High sequence conservation is observed even between distantly related species.
- DING proteins exhibit heterogeneous biological activities and bind to phosphate and other ligands, with some implicated in pathologies.
Conclusions:
- DING proteins represent a highly conserved and functionally diverse protein family with potential roles in disease.
- Further research is needed to fully elucidate the functions and mechanisms of various DING proteins.
- This review consolidates current knowledge, paving the way for future investigations into DING protein biology.
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