A heme-binding aspartic proteinase from the eggs of the hard tick Boophilus microplus
Autor(a) principal: | |
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Data de Publicação: | 2000 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://repositorio.unifesp.br/handle/11600/26383 http://dx.doi.org/10.1074/jbc.M005675200 |
Resumo: | An aspartic proteinase that binds heme with a 1:1 stoichiometry was isolated and cloned from the eggs of the cattle tick Boophilus microplus. This proteinase, herein named THAP (tick heme-binding aspartic proteinase) showed pepstatin-sensitive hydrolytic activity against several peptide and protein substrates, Although hemoglobin was a good substrate for THAP, low proteolytic activity was observed against globin devoid of the heme prosthetic group. Hydrolysis of globin by THAP increased as increasing amounts of heme were added to globin, with maximum activation at a heme-to-globin 1:1 ratio. Further additions of heme to the reaction medium inhibited proteolysis, back to a level similar to that observed against globin alone. the addition of heme did not change THAP activity toward a synthetic peptide or against ribonuclease, a non-hemeprotein substrate. the major storage protein of tick eggs, vitellin (VT), the probable physiological substrate of THAP, is a hemeprotein. Hydrolysis of VT by THAP was also inhibited by the addition of heme to the incubation media. Taken together, our results suggest that THAP uses heme bound to VT as a docking site to increase specificity and regulate VT degradation according to heme availability. |
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Repositório Institucional da UNIFESP |
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Sorgine, MHFLogullo, C.Zingali, R. B.Paiva-Silva, G. O.Juliano, Luiz [UNIFESP]Oliveira, P. L.Universidade Federal do Rio de Janeiro (UFRJ)Universidade Federal de São Paulo (UNIFESP)Universidade Federal Fluminense (UFF)2016-01-24T12:31:10Z2016-01-24T12:31:10Z2000-09-15Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 275, n. 37, p. 28659-28665, 2000.0021-9258http://repositorio.unifesp.br/handle/11600/26383http://dx.doi.org/10.1074/jbc.M00567520010.1074/jbc.M005675200WOS:000089330700044An aspartic proteinase that binds heme with a 1:1 stoichiometry was isolated and cloned from the eggs of the cattle tick Boophilus microplus. This proteinase, herein named THAP (tick heme-binding aspartic proteinase) showed pepstatin-sensitive hydrolytic activity against several peptide and protein substrates, Although hemoglobin was a good substrate for THAP, low proteolytic activity was observed against globin devoid of the heme prosthetic group. Hydrolysis of globin by THAP increased as increasing amounts of heme were added to globin, with maximum activation at a heme-to-globin 1:1 ratio. Further additions of heme to the reaction medium inhibited proteolysis, back to a level similar to that observed against globin alone. the addition of heme did not change THAP activity toward a synthetic peptide or against ribonuclease, a non-hemeprotein substrate. the major storage protein of tick eggs, vitellin (VT), the probable physiological substrate of THAP, is a hemeprotein. Hydrolysis of VT by THAP was also inhibited by the addition of heme to the incubation media. Taken together, our results suggest that THAP uses heme bound to VT as a docking site to increase specificity and regulate VT degradation according to heme availability.Univ Fed Rio de Janeiro, Ctr Ciencias Saude, Inst Ciencias Biomed, Dept Bioquim Med, BR-21910590 Rio de Janeiro, BrazilUNIFESP, Escola Paulista Med, Dept Biofis, BR-04044020 São Paulo, BrazilUniv Fed Fluminense, Inst Biol, Dept Biol Celular & Mol, BR-24001970 Niteroi, RJ, BrazilUNIFESP, Escola Paulista Med, Dept Biofis, BR-04044020 São Paulo, BrazilWeb of Science28659-28665engAmer Soc Biochemistry Molecular Biology IncJournal of Biological ChemistryA heme-binding aspartic proteinase from the eggs of the hard tick Boophilus microplusinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP11600/263832021-09-29 11:23:43.942metadata only accessoai:repositorio.unifesp.br:11600/26383Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652023-05-25T12:17:33.113073Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
A heme-binding aspartic proteinase from the eggs of the hard tick Boophilus microplus |
title |
A heme-binding aspartic proteinase from the eggs of the hard tick Boophilus microplus |
spellingShingle |
A heme-binding aspartic proteinase from the eggs of the hard tick Boophilus microplus Sorgine, MHF |
title_short |
A heme-binding aspartic proteinase from the eggs of the hard tick Boophilus microplus |
title_full |
A heme-binding aspartic proteinase from the eggs of the hard tick Boophilus microplus |
title_fullStr |
A heme-binding aspartic proteinase from the eggs of the hard tick Boophilus microplus |
title_full_unstemmed |
A heme-binding aspartic proteinase from the eggs of the hard tick Boophilus microplus |
title_sort |
A heme-binding aspartic proteinase from the eggs of the hard tick Boophilus microplus |
author |
Sorgine, MHF |
author_facet |
Sorgine, MHF Logullo, C. Zingali, R. B. Paiva-Silva, G. O. Juliano, Luiz [UNIFESP] Oliveira, P. L. |
author_role |
author |
author2 |
Logullo, C. Zingali, R. B. Paiva-Silva, G. O. Juliano, Luiz [UNIFESP] Oliveira, P. L. |
author2_role |
author author author author author |
dc.contributor.institution.none.fl_str_mv |
Universidade Federal do Rio de Janeiro (UFRJ) Universidade Federal de São Paulo (UNIFESP) Universidade Federal Fluminense (UFF) |
dc.contributor.author.fl_str_mv |
Sorgine, MHF Logullo, C. Zingali, R. B. Paiva-Silva, G. O. Juliano, Luiz [UNIFESP] Oliveira, P. L. |
description |
An aspartic proteinase that binds heme with a 1:1 stoichiometry was isolated and cloned from the eggs of the cattle tick Boophilus microplus. This proteinase, herein named THAP (tick heme-binding aspartic proteinase) showed pepstatin-sensitive hydrolytic activity against several peptide and protein substrates, Although hemoglobin was a good substrate for THAP, low proteolytic activity was observed against globin devoid of the heme prosthetic group. Hydrolysis of globin by THAP increased as increasing amounts of heme were added to globin, with maximum activation at a heme-to-globin 1:1 ratio. Further additions of heme to the reaction medium inhibited proteolysis, back to a level similar to that observed against globin alone. the addition of heme did not change THAP activity toward a synthetic peptide or against ribonuclease, a non-hemeprotein substrate. the major storage protein of tick eggs, vitellin (VT), the probable physiological substrate of THAP, is a hemeprotein. Hydrolysis of VT by THAP was also inhibited by the addition of heme to the incubation media. Taken together, our results suggest that THAP uses heme bound to VT as a docking site to increase specificity and regulate VT degradation according to heme availability. |
publishDate |
2000 |
dc.date.issued.fl_str_mv |
2000-09-15 |
dc.date.accessioned.fl_str_mv |
2016-01-24T12:31:10Z |
dc.date.available.fl_str_mv |
2016-01-24T12:31:10Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 275, n. 37, p. 28659-28665, 2000. |
dc.identifier.uri.fl_str_mv |
http://repositorio.unifesp.br/handle/11600/26383 http://dx.doi.org/10.1074/jbc.M005675200 |
dc.identifier.issn.none.fl_str_mv |
0021-9258 |
dc.identifier.doi.none.fl_str_mv |
10.1074/jbc.M005675200 |
dc.identifier.wos.none.fl_str_mv |
WOS:000089330700044 |
identifier_str_mv |
Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 275, n. 37, p. 28659-28665, 2000. 0021-9258 10.1074/jbc.M005675200 WOS:000089330700044 |
url |
http://repositorio.unifesp.br/handle/11600/26383 http://dx.doi.org/10.1074/jbc.M005675200 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.none.fl_str_mv |
Journal of Biological Chemistry |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
28659-28665 |
dc.publisher.none.fl_str_mv |
Amer Soc Biochemistry Molecular Biology Inc |
publisher.none.fl_str_mv |
Amer Soc Biochemistry Molecular Biology Inc |
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 |
|
_version_ |
1783460272690692096 |