Di Maro Antimo, De Maio Anna, Castellano Sabrina, Parente Augusto, Farina Benedetta, Faraone-Mennella Maria Rosaria
Department of Life Sciences, Faculty of Sciences M.F.N., Second University of Naples, Via Vivadi 45, I-81100 Caserta, Italy.
Biol Chem. 2009 Jan;390(1):27-30. doi: 10.1515/BC.2009.006.
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.
经生化鉴定为聚(ADP - 核糖)聚合酶样酶的嗜硫叶菌热蛋白的部分氨基酸序列与DING蛋白的序列重叠。这组广泛存在于动物、植物和真细菌中的蛋白质具有一个特征性且高度保守的N端,即DINGGGATL。嗜硫叶菌热酶的N端区域序列以及所分析的胰蛋白酶肽段与数据库中大多数DING蛋白具有高度相似性。这是来自嗜硫叶菌来源的DING蛋白的首个实例。