Metacaspase 2 of Trypanosoma brucei is a calcium-dependent cysteine peptidase active without processing

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Date
2007-12-11Author
Moss, Catherine X.
Westrop, Gareth D.
Juliano, Luiz [UNIFESP]
Coombs, Graham H.
Mottram, Jeremy C.
Type
ArtigoISSN
0014-5793Is part of
Febs LettersDOI
10.1016/j.febslet.2007.11.009Metadata
Show full item recordAbstract
Metacaspases are cysteine peptidases that are distantly related to the caspases, for which proteolytic processing is central to their activation. Here, we show that recombinant metacaspase 2 (MCA2) from Trypanosoma brucei has arginine/lysine-specific, Ca2+-dependent proteolytic activity. Autocatalytic processing of MCA2 occurred after Lys55 and Lys268; however, this was shown not to be required for the enzyme to be proteolytically active. the necessity of Ca2+, but not processing, for MCA2 enzymatic activity clearly distinguishes MCA2 from the caspases and would be consistent with different physiological roles. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Citation
Febs Letters. Amsterdam: Elsevier B.V., v. 581, n. 29, p. 5635-5639, 2007.Keywords
caspasemetacaspase
cysteine protease
calcium
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