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

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, Ca 2+-dependent proteolytic activity. Autocataly...

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Bibliographic Details
Published in:FEBS letters 2007-12, Vol.581 (29), p.5635-5639
Main Authors: Moss, Catherine X., Westrop, Gareth D., Juliano, Luiz, Coombs, Graham H., Mottram, Jeremy C.
Format: Article
Language:English
Subjects:
7-amino-4-methylcoumarin
AMC
Animals
Arginine - metabolism
Calcium
Calcium - metabolism
Caspase
Caspases - metabolism
Cysteine Endopeptidases - metabolism
Cysteine protease
EF-Tu
elongation factor Tu
glutathione S-transferase
GST
Lysine - metabolism
MCA
Metacaspase
Mutagenesis, Site-Directed
PCD
programmed cell death
Protozoan Proteins - metabolism
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
TLCK
tosyl-lysyl-chloromethylketone
Trypanosoma brucei
Trypanosoma brucei brucei - enzymology
Trypanosoma brucei brucei - metabolism
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Summary: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, Ca 2+-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 Ca 2+, but not processing, for MCA2 enzymatic activity clearly distinguishes MCA2 from the caspases and would be consistent with different physiological roles.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2007.11.009