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

Detalhes bibliográficos
Autor(a) principal: Moss, Catherine X.
Data de Publicação: 2007
Outros Autores: Westrop, Gareth D., Juliano, Luiz [UNIFESP], Coombs, Graham H., Mottram, Jeremy C.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNIFESP
dARK ID: ark:/48912/0013000000v4k
Texto Completo: http://dx.doi.org/10.1016/j.febslet.2007.11.009
http://repositorio.unifesp.br/handle/11600/30210
Resumo: 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.
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spelling Metacaspase 2 of Trypanosoma brucei is a calcium-dependent cysteine peptidase active without processingcaspasemetacaspasecysteine proteasecalciumMetacaspases 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.Univ Glasgow, Inst Biomed & Life Sci, Wellcome Ctr Mol Parasitol, Glasgow G12 8TA, Lanark, ScotlandUniv Glasgow, Inst Biomed & Life Sci, Div Infect & Immunity, Glasgow G12 8TA, Lanark, ScotlandUniv Strathclyde, Strathclyde Inst Pharm & Biomed Sci, Glasgow G4 0NR, Lanark, ScotlandUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biofis, São Paulo, BrazilUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biofis, São Paulo, BrazilWeb of ScienceElsevier B.V.Univ GlasgowUniv StrathclydeUniversidade Federal de São Paulo (UNIFESP)Moss, Catherine X.Westrop, Gareth D.Juliano, Luiz [UNIFESP]Coombs, Graham H.Mottram, Jeremy C.2016-01-24T13:49:17Z2016-01-24T13:49:17Z2007-12-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion5635-5639application/pdfhttp://dx.doi.org/10.1016/j.febslet.2007.11.009Febs Letters. Amsterdam: Elsevier B.V., v. 581, n. 29, p. 5635-5639, 2007.10.1016/j.febslet.2007.11.009WOS000253488000015.pdf0014-5793http://repositorio.unifesp.br/handle/11600/30210WOS:000253488000015ark:/48912/0013000000v4kengFebs Lettersinfo:eu-repo/semantics/openAccesshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policyreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2024-07-31T08:09:30Zoai:repositorio.unifesp.br/:11600/30210Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652024-12-11T19:49:21.869389Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false
dc.title.none.fl_str_mv Metacaspase 2 of Trypanosoma brucei is a calcium-dependent cysteine peptidase active without processing
title Metacaspase 2 of Trypanosoma brucei is a calcium-dependent cysteine peptidase active without processing
spellingShingle Metacaspase 2 of Trypanosoma brucei is a calcium-dependent cysteine peptidase active without processing
Moss, Catherine X.
caspase
metacaspase
cysteine protease
calcium
title_short Metacaspase 2 of Trypanosoma brucei is a calcium-dependent cysteine peptidase active without processing
title_full Metacaspase 2 of Trypanosoma brucei is a calcium-dependent cysteine peptidase active without processing
title_fullStr Metacaspase 2 of Trypanosoma brucei is a calcium-dependent cysteine peptidase active without processing
title_full_unstemmed Metacaspase 2 of Trypanosoma brucei is a calcium-dependent cysteine peptidase active without processing
title_sort Metacaspase 2 of Trypanosoma brucei is a calcium-dependent cysteine peptidase active without processing
author Moss, Catherine X.
author_facet Moss, Catherine X.
Westrop, Gareth D.
Juliano, Luiz [UNIFESP]
Coombs, Graham H.
Mottram, Jeremy C.
author_role author
author2 Westrop, Gareth D.
Juliano, Luiz [UNIFESP]
Coombs, Graham H.
Mottram, Jeremy C.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Univ Glasgow
Univ Strathclyde
Universidade Federal de São Paulo (UNIFESP)
dc.contributor.author.fl_str_mv Moss, Catherine X.
Westrop, Gareth D.
Juliano, Luiz [UNIFESP]
Coombs, Graham H.
Mottram, Jeremy C.
dc.subject.por.fl_str_mv caspase
metacaspase
cysteine protease
calcium
topic caspase
metacaspase
cysteine protease
calcium
description 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.
publishDate 2007
dc.date.none.fl_str_mv 2007-12-11
2016-01-24T13:49:17Z
2016-01-24T13:49:17Z
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1016/j.febslet.2007.11.009
Febs Letters. Amsterdam: Elsevier B.V., v. 581, n. 29, p. 5635-5639, 2007.
10.1016/j.febslet.2007.11.009
WOS000253488000015.pdf
0014-5793
http://repositorio.unifesp.br/handle/11600/30210
WOS:000253488000015
dc.identifier.dark.fl_str_mv ark:/48912/0013000000v4k
url http://dx.doi.org/10.1016/j.febslet.2007.11.009
http://repositorio.unifesp.br/handle/11600/30210
identifier_str_mv Febs Letters. Amsterdam: Elsevier B.V., v. 581, n. 29, p. 5635-5639, 2007.
10.1016/j.febslet.2007.11.009
WOS000253488000015.pdf
0014-5793
WOS:000253488000015
ark:/48912/0013000000v4k
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Febs Letters
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
eu_rights_str_mv openAccess
rights_invalid_str_mv http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.format.none.fl_str_mv 5635-5639
application/pdf
dc.publisher.none.fl_str_mv Elsevier B.V.
publisher.none.fl_str_mv Elsevier B.V.
dc.source.none.fl_str_mv reponame:Repositório Institucional da UNIFESP
instname:Universidade Federal de São Paulo (UNIFESP)
instacron:UNIFESP
instname_str Universidade Federal de São Paulo (UNIFESP)
instacron_str UNIFESP
institution UNIFESP
reponame_str Repositório Institucional da UNIFESP
collection Repositório Institucional da UNIFESP
repository.name.fl_str_mv Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)
repository.mail.fl_str_mv biblioteca.csp@unifesp.br
_version_ 1818602378154213376

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