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

Biol Chem. 2009 Jan;390(1):27-30. doi: 10.1515/BC.2009.006.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate / metabolism*
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / metabolism
  • Conserved Sequence*
  • Humans
  • Molecular Sequence Data
  • Poly(ADP-ribose) Polymerases / chemistry*
  • Poly(ADP-ribose) Polymerases / metabolism
  • Sequence Alignment
  • Sulfolobus solfataricus / enzymology*

Substances

  • Archaeal Proteins
  • Adenosine Diphosphate
  • Poly(ADP-ribose) Polymerases