کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1179089 | 962755 | 2008 | 9 صفحه PDF | دانلود رایگان |
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.
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1784, Issue 9, September 2008, Pages 1256–1264