A novel serralysin metalloprotease from Deinococcus radiodurans

Basu, Bhakti ; Apte, Shree Kumar (2008) A novel serralysin metalloprotease from Deinococcus radiodurans Biochimica et Biophysica Acta (BBA): Proteins & Proteomics, 1784 (9). pp. 1256-1264. ISSN 1570-9639

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/S15709...

Related URL: http://dx.doi.org/10.1016/j.bbapap.2008.05.009


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.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Deinococcus; Serralysin-Like Extracellular Metalloprotease; Zn+2/Ca+2-Dependency
ID Code:756
Deposited On:25 Sep 2010 04:47
Last Modified:05 Jan 2011 06:41

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