A novel serralysin metalloprotease from Deinococcus radiodurans.

A novel serralysin metalloprotease from Deinococcus radiodurans. Research Abstract Details 

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A novel serralysin metalloprotease from Deinococcus radiodurans. Abstract Text:

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.

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A novel serralysin metalloprotease from Deinococcus radiodurans. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Biochimica et biophysica acta

VOLUME: 1784

Page Numbers: 1256-64

Journal Abbreviation: Biochim. Biophys. Acta

ISSN: 0006-3002

DAY: 6

MONTH: 06

YEAR: 2008

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LANGUAGE: eng

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Grant and Affiliation Information for A novel serralysin metalloprotease from Deinococcus radiodurans.

AFFILIATION: Molecular Biology Division, Bhabha Atomic Research Centre, Mumbai - 400085, India.

Country: Netherlands

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MEDLINETA: Biochim Biophys Acta

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