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DING Proteins Extend to the Extremophilic World
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 con...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7922408/ https://www.ncbi.nlm.nih.gov/pubmed/33670786 http://dx.doi.org/10.3390/ijms22042035 |
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author | Porzio, Elena Faraone Mennella, Maria Rosaria Manco, Giuseppe |
author_facet | Porzio, Elena Faraone Mennella, Maria Rosaria Manco, Giuseppe |
author_sort | Porzio, Elena |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7922408 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-79224082021-03-03 DING Proteins Extend to the Extremophilic World Porzio, Elena Faraone Mennella, Maria Rosaria Manco, Giuseppe Int J Mol Sci Review 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. MDPI 2021-02-18 /pmc/articles/PMC7922408/ /pubmed/33670786 http://dx.doi.org/10.3390/ijms22042035 Text en © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Porzio, Elena Faraone Mennella, Maria Rosaria Manco, Giuseppe DING Proteins Extend to the Extremophilic World |
title | DING Proteins Extend to the Extremophilic World |
title_full | DING Proteins Extend to the Extremophilic World |
title_fullStr | DING Proteins Extend to the Extremophilic World |
title_full_unstemmed | DING Proteins Extend to the Extremophilic World |
title_short | DING Proteins Extend to the Extremophilic World |
title_sort | ding proteins extend to the extremophilic world |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7922408/ https://www.ncbi.nlm.nih.gov/pubmed/33670786 http://dx.doi.org/10.3390/ijms22042035 |
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