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- Title
Comparison of the DING protein from the archaeon <italic>Sulfolobus solfataricus</italic> with human phosphate-binding protein and <italic>Pseudomonas fluorescence</italic> DING counterparts.
- Authors
Porzio, Elena; De Maio, Anna; Ricciardi, Teresa; Mistretta, Carmela; Manco, Giuseppe; Faraone-Mennella, Maria Rosaria
- Abstract
DING proteins represent a new group of 40 kDa-related members, ubiquitous in living organisms. The family also include the DING protein from <italic>Sulfolobus solfataricus</italic>, functionally related to poly(ADP-ribose) polymerases. Here, the archaeal protein has been compared with the <italic>human</italic> Phosphate-Binding Protein and the <italic>Pseudomonas fluorescence</italic> DING enzyme, by enzyme assays and immune cross-reactivity. Surprisingly, as the <italic>Sulfolobus</italic> enzyme, the <italic>Human</italic> and <italic>Pseudomonas</italic> proteins display poly(ADP-ribose) polymerase activity, whereas a phosphatase activity was only present in <italic>Sulfolobus</italic> and human protein, despite the conserved phosphate-binding site residues in <italic>Pseudomonas</italic> DING. All proteins were positive to anti-DING antibodies and gave a comparable pattern of anti-poly(ADP-ribose) polymerase immunoreactivity with two bands, at around 40 kDa and roughly at the double of this molecular mass. The latter signal was present in all <italic>Sulfolobus</italic> enzyme preparations and proved not due to either a contaminant or a precursor protein, but likely being a dimeric form of the 40 kDa polypeptide. The common immunological and partly enzymatic behavior linking human, <italic>Pseudomonas</italic> and <italic>Sulfolobus</italic> DING proteins, makes the archaeal protein an important model system to investigate DING protein function and evolution within the cell.
- Subjects
SULFOLOBUS solfataricus; BACTERIAL proteins; ARCHAEBACTERIAL proteins; PSEUDOMONAS; POLYMERASES
- Publication
Extremophiles, 2018, Vol 22, Issue 2, p177
- ISSN
1431-0651
- Publication type
Article
- DOI
10.1007/s00792-017-0985-4