The ADP-ribosylating thermozyme from Sulfolobus solfataricus is a DING protein.
The partial amino acid sequence of the sulfolobal thermoprotein biochemically characterized as poly(ADP-ribose)polymerase-like enzyme overlaps those of DING proteins. This group of proteins, widely occurring in animals, plants and eubacteria, shows a characteristic and highly conserved N-terminus, DINGGGATL. The sequence of the N-terminal region and of the analyzed tryptic peptides of the sulfolobal thermozyme shows a high similarity with most of the DING proteins from databases. This is the first example of a DING protein from a sulfolobal source.
Di Maro
Antimo
A
Department of Life Sciences, Faculty of Sciences M.F.N., Second University of Naples, Via Vivadi 45, I-81100 Caserta, Italy.
De Maio
Anna
A
Castellano
Sabrina
S
Parente
Augusto
A
Farina
Benedetta
B
Faraone-Mennella
Maria Rosaria
MR
D000244:Adenosine Diphosphate / Q000378:metabolism*; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism; D017124:Conserved Sequence; D006801:Humans; D008969:Molecular Sequence Data; D011065:Poly(ADP-ribose) Polymerases / Q000737:chemistry* / Q000378:metabolism; D016415:Sequence Alignment; D048229:Sulfolobus solfataricus / Q000201:enzymology*
D019843:Archaeal Proteins; D000244:Adenosine Diphosphate; D011065:Poly(ADP-ribose) Polymerases