The DING family of proteins: ubiquitous in eukaryotes, but where are the genes?

Berna, Anne; Scott, Kevin R.; Chabrière, Éric; Bernier, François

doi:10.1002/bies.200800174

Cited by 31 publications

(41 citation statements)

References 68 publications

(106 reference statements)

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“…Moreover, despite the biochemical properties allowed to correlate PARPSso to PARP enzymes, a first BLAST research of purified PARPSso towards classic PARPs was not fruitful: the structural analysis indicated that the sulfolobal enzyme had a different structure, resembling a new group of proteins, the DING proteins, Figure 2 [34][35][36].…”

Section: Parpsso Belongs To the Ding Protein Familymentioning

confidence: 99%

“…They belong to the superfamily of bacterial phosphate-binding proteins [35]. The phosphate-binding site is strongly conserved and comprises eight conserved or conservatively-substituted residues, responsible to hydrogen-bind the phosphate ion with high affinity [35].…”

Section: Parpsso Belongs To the Ding Protein Familymentioning

confidence: 99%

“…The peculiarity of these proteins is that they have beenserendipitously discovered as members of the DING group [35,36]. DING proteins have been mostly identified thanks to their biological functions and their number is expected to increase due to the possibility that some of them, perhaps already studied for their functions, are not structurally identified as DING proteins yet [35].…”

Section: Parpsso Belongs To the Ding Protein Familymentioning

confidence: 99%

“…DING proteins have been mostly identified thanks to their biological functions and their number is expected to increase due to the possibility that some of them, perhaps already studied for their functions, are not structurally identified as DING proteins yet [35]. The high similarity of amino acid sequences and some highly conserved domains (phosphate binding sites) from prokaryotes to eukaryotes are surprising [35,36].…”

Section: Parpsso Belongs To the Ding Protein Familymentioning

confidence: 99%

“…The high similarity of amino acid sequences and some highly conserved domains (phosphate binding sites) from prokaryotes to eukaryotes are surprising [35,36]. Surprising is also the diversity of activities displayed by DING proteins from different sources;among others apolipoprotein, protease, alkaline phosphatase, phosphodiesterase, nucleotidase, and secretion proteins have been identified and reviewed in [35,36].…”

Section: Parpsso Belongs To the Ding Protein Familymentioning

confidence: 99%

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The Dichotomy of the Poly(ADP-Ribose) Polymerase-Like Thermozyme from Sulfolobus solfataricus

Faraone-Mennella¹,

Rosaria²

2018

Challenges

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Abstract:The first evidence of an ADP-ribosylating activity in Archaea was obtained in Sulfolobus solfataricus(strain MT-4) where a poly(ADP-ribose) polymerase (PARP)-like thermoprotein, defined with the acronymous PARPSso, was found. Similarly to the eukaryotic counterparts PARPSso cleaves beta-nicotinamide adenine dinucleotide to synthesize oligomers of ADP-ribose; cross-reacts with polyclonal anti-PARP-1 catalytic site antibodies; binds DNA. The main differences rely on the molecular mass (46.5 kDa) and the thermophily of PARPSso which works at 80 • C. Despite the biochemical properties that allow correlating it to PARP enzymes, the N-terminal and partial amino acid sequences available suggest that PARPSso belongs to a different group of enzymes, the DING proteins, an item discussed in detail in this review.This finding makes PARPSso the first example of a DING protein in Archaea and extends the existence of DING proteins into all the biological kingdoms. PARPSsohas a cell peripheral localization, along with the edge of the cell membrane. The ADP-ribosylation reaction is reverted by a poly(ADP-ribose) glycohydrolase-like activity, able to use the eukaryotic poly(ADP-ribose) as a substrate too. Here we overview the research of (ADP-ribosyl)ation in Sulfolobus solfataricus in the past thirty years and discuss the features of PARPSso common with the canonical poly(ADP-ribose) polymerases, and the structure fitting with that of DING proteins.

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Section: Parpsso Belongs To the Ding Protein Familymentioning

confidence: 99%

Section: Parpsso Belongs To the Ding Protein Familymentioning

confidence: 99%

Section: Parpsso Belongs To the Ding Protein Familymentioning

confidence: 99%

Section: Parpsso Belongs To the Ding Protein Familymentioning

confidence: 99%

Section: Parpsso Belongs To the Ding Protein Familymentioning

confidence: 99%

See 3 more Smart Citations

The Dichotomy of the Poly(ADP-Ribose) Polymerase-Like Thermozyme from Sulfolobus solfataricus

Faraone-Mennella¹,

Rosaria²

2018

Challenges

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Suppression of HIV‐1 transcriptional elongation by a DING phosphatase

Darbinian

Gomberg

Mullen

et al. 2011

J of Cellular Biochemistry

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HIV-1 gene transcription is controlled by the cooperation of viral and host factors which bind to specific DNA sequences within the viral promoter spanning the long terminal repeat, LTR. Previously we showed that the St. John's Wort DING phosphatase, p27SJ, suppresses HIV-1 gene transcription by binding to the viral protein Tat and preventing its nuclear import. Here, we describe the inhibitory effect of p27SJ on the phosphorylation of the C-terminal domain (CTD) of RNA polymerase II (RNAPII). This inhibition leads to the suppression of the association of RNAPII with the LTR. Inhibition of binding of RNAPII to LTR by p27SJ resulted in the suppression of LTR transcription elongation and a decrease in LTR transcriptional activity. Another form of the St. John's Wort DING phosphatase, p38SJ, also suppressed binding of RNAPII to the LTR, reduced transcription elongation and was even more powerful than p27SJ in inhibiting the transcriptional activity of the LTR. Our data suggest a possible mechanism by which the p27SJ/p38SJ DING phosphatase can regulate HIV-1 LTR expression by inhibiting phosphorylation of the CTD of RNAPII and suppressing LTR transcription elongation.

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The DING Family of Phosphate Binding Proteins in Inflammatory Diseases

González

Elias

Chabrière

2014

Advances in Experimental Medicine and Biology

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Human paraoxonase 1 (hPON-1) is a protein that has been studied in relation to its antioxidant and anti-atherosclerotic properties. Despite extensive studies, the molecular mechanisms responsible for its functional properties remain unclear. During the last decade, a new partner of hPON-1 has been identified. Hidden for a long time because of a similar molecular weight with hPON-1, this protein, termed human phosphate-binding protein (HPBP), may contribute to the biological functions of hPON-1. Belonging to the DING protein, a sub-family of phosphate binding proteins (PBP or pstS), HPBP stabilizes hPON-1 and might prevent calcification of arteries in case of advance atherosclerosis. The role of other DING proteins in some calcification processes (i.e. nephrolithiasis) and the identification of HPBP in the atheroma plaque support this hypothesis. Nevertheless, the relevance of hPON-1/HPBP as well as the molecular determinants in atherosclerosis remains to be elucidated.

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The DING family of proteins: ubiquitous in eukaryotes, but where are the genes?

Cited by 31 publications

References 68 publications

The Dichotomy of the Poly(ADP-Ribose) Polymerase-Like Thermozyme from Sulfolobus solfataricus

The Dichotomy of the Poly(ADP-Ribose) Polymerase-Like Thermozyme from Sulfolobus solfataricus

Suppression of HIV‐1 transcriptional elongation by a DING phosphatase

The DING Family of Phosphate Binding Proteins in Inflammatory Diseases

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