In this paper it was demonstrated that 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.

The ADP-ribosylating thermozyme from Sulfolobus solfataricus is a DING protein / Di Maro, A; DE MAIO, Anna; Castellano, S; Parente, A; Farina, B; FARAONE MENNELLA, MARIA ROSARIA. - In: BIOLOGICAL CHEMISTRY. - ISSN 1431-6730. - ELETTRONICO. - 390:1(2009), pp. 27-30.

The ADP-ribosylating thermozyme from Sulfolobus solfataricus is a DING protein.

DE MAIO, ANNA;FARAONE MENNELLA, MARIA ROSARIA
2009

Abstract

In this paper it was demonstrated that 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.
2009
The ADP-ribosylating thermozyme from Sulfolobus solfataricus is a DING protein / Di Maro, A; DE MAIO, Anna; Castellano, S; Parente, A; Farina, B; FARAONE MENNELLA, MARIA ROSARIA. - In: BIOLOGICAL CHEMISTRY. - ISSN 1431-6730. - ELETTRONICO. - 390:1(2009), pp. 27-30.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/333368
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