A novel serralysin metalloprotease from Deinococcus radiodurans
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- 作者：Bhakti Basu ; Shree Kumar Apte
- 关键词：Deinococcus ; Serralysin-like extracellular metalloprotease ; Zn+2/Ca+2-dependency
- 刊名：Biochimica et Biophysica Acta - Proteins and Proteomics
- 出版年：2008
- 出版时间：September 2008
- 年：2008
- 卷：1784
- 期：9
- 页码：1256-1264
- 全文大小：2110 K
文摘
A hypothetical protein (DR2310) from the radiation resistant organism Deinococcus radiodurans harbors highly conserved Zn+2-binding (HEXXH) domain and Met-turn (SVMSY), characteristic of the serralysin family of secreted metalloproteases from Gram negative bacteria. Deletion mutagenesis of DR2310 confirmed that the ORF is expressed in Deinococcus radiodurans as a secreted protease of 85 kDa. Biochemical analysis revealed DR2310 to be a Ca+2 and Zn+2-requiring metalloprotease. Unique features such as a long N-terminus, replacement of the highly conserved C-terminal glycine rich Ca+2-binding repeats with a single N-terminal aspartate rich eukaryotic thrombospondin type-3 Ca+2-binding repeat and absence of C-terminal secretion signals make it a novel member of serralysin family. This is the first report of a functional serralysin family metalloprotease from a Gram positive organism.