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...
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2021-02-01
|
| Series: | International Journal of Molecular Sciences |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1422-0067/22/4/2035 |
| _version_ | 1797396031532433408 |
|---|---|
| author | Elena Porzio Maria Rosaria Faraone Mennella Giuseppe Manco |
| author_facet | Elena Porzio Maria Rosaria Faraone Mennella Giuseppe Manco |
| author_sort | Elena Porzio |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-03-09T00:45:26Z |
| format | Article |
| id | doaj.art-2865a9ef99c6463d9f35484c1d325c7b |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T00:45:26Z |
| publishDate | 2021-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-2865a9ef99c6463d9f35484c1d325c7b2023-12-11T17:33:36ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-02-01224203510.3390/ijms22042035DING Proteins Extend to the Extremophilic WorldElena Porzio0Maria Rosaria Faraone Mennella1Giuseppe Manco2Institute of Biochemistry and Cell Biology, CNR, Via P. Castellino 111, 80131 Naples, ItalyDepartment of Biology, Polytechnic School of Basic Sciences, University of Naples “Federico II”, 80126 Naples, ItalyInstitute of Biochemistry and Cell Biology, CNR, Via P. Castellino 111, 80131 Naples, ItalyThe 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.https://www.mdpi.com/1422-0067/22/4/2035DING proteinPARPSsoArchaeaprokaryoteseukaryotesextremophiles |
| spellingShingle | Elena Porzio Maria Rosaria Faraone Mennella Giuseppe Manco DING Proteins Extend to the Extremophilic World International Journal of Molecular Sciences DING protein PARPSso Archaea prokaryotes eukaryotes extremophiles |
| 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 | DING protein PARPSso Archaea prokaryotes eukaryotes extremophiles |
| url | https://www.mdpi.com/1422-0067/22/4/2035 |
| work_keys_str_mv | AT elenaporzio dingproteinsextendtotheextremophilicworld AT mariarosariafaraonemennella dingproteinsextendtotheextremophilicworld AT giuseppemanco dingproteinsextendtotheextremophilicworld |