| Literature DB >> 19007307 |
Antimo Di Maro1, Anna De Maio, Sabrina Castellano, Augusto Parente, Benedetta Farina, Maria Rosaria Faraone-Mennella.
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.Entities:
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Year: 2009 PMID: 19007307 DOI: 10.1515/BC.2009.006
Source DB: PubMed Journal: Biol Chem ISSN: 1431-6730 Impact factor: 3.915