Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Porzio, Elena, Faraone Mennella, Maria Rosaria, Manco, Giuseppe
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
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
_version_ 1783658682665402368
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
work_keys_str_mv AT porzioelena dingproteinsextendtotheextremophilicworld
AT faraonemennellamariarosaria dingproteinsextendtotheextremophilicworld
AT mancogiuseppe dingproteinsextendtotheextremophilicworld