Preliminary study of the enzyme ubiquitin carboxylterminal hydrolase 14 (UBP6) in Giardia intestinalis: structural bioinformatic analysis and transcriptional profile during encystation

This paper presents a combined approachwith two aims. The first is to analyze thereported sequence of the enzyme ubiquitincarboxyl-terminal hydrolase 14 of Giardiaintestinalis (UBP6) through computationalmethods to find components related withits hypothetical function. The second isto determine if t...

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Autores:
Alvarado, Magda E
González, Camila A
Wasserman, Moisés
Rubiano, Claudia C
Tipo de recurso:
Article of journal
Fecha de publicación:
2014
Institución:
Universidad Nacional de Colombia
Repositorio:
Universidad Nacional de Colombia
Idioma:
spa
OAI Identifier:
oai:repositorio.unal.edu.co:unal/66323
Acceso en línea:
https://repositorio.unal.edu.co/handle/unal/66323
http://bdigital.unal.edu.co/67347/
Palabra clave:
54 Química y ciencias afines / Chemistry
deubiquitinating enzymes
ubiquitin
Giardia intestinalis
encystation
Rights
openAccess
License
Atribución-NoComercial 4.0 Internacional
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oai_identifier_str oai:repositorio.unal.edu.co:unal/66323
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network_name_str Universidad Nacional de Colombia
repository_id_str
spelling Atribución-NoComercial 4.0 InternacionalDerechos reservados - Universidad Nacional de Colombiahttp://creativecommons.org/licenses/by-nc/4.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Alvarado, Magda Ecd9a4a37-a9a2-42e2-917a-9f2438186a07300González, Camila A810fc619-0e3d-4d76-894e-6ca54a5528c3300Wasserman, Moisés0284b745-5934-4050-bf95-03d2fa912277300Rubiano, Claudia C89958285-883d-493b-8454-f489f11abef63002019-07-03T01:54:32Z2019-07-03T01:54:32Z2014-05-01ISSN: 2357-3791https://repositorio.unal.edu.co/handle/unal/66323http://bdigital.unal.edu.co/67347/This paper presents a combined approachwith two aims. The first is to analyze thereported sequence of the enzyme ubiquitincarboxyl-terminal hydrolase 14 of Giardiaintestinalis (UBP6) through computationalmethods to find components related withits hypothetical function. The second isto determine if the protein-coding gene isexpressed in G. intestinalis and, if such isthe case, also determine its transcriptionpattern along the life cycle of the parasite. Itwas established that the protein belongs tothe family of Cys-dependent deubiquitinasesand more specifically to ubiquitin specificproteases (USPs). Moreover, the catalyticcenter with the complete triad as well astypical features of the USP motif were alsoidentified. Since the computational findingssuggest that the enzyme could be functional,reverse transcription coupled to PCR wasused as a first approach to establish if in factthe coding gene is expressed in the parasite.Interestingly, it was found not only thatthe gene is expressed, but also that thereis a transcription variation along the lifecycle of the parasite. These two findings arethe starting point for further studies sincethey tentatively suggest that this enzymecould be involved in the protein turnoverthat occurs during parasite encystation.Although preliminary, this study is the firstreport concerning the study of a specificdeubiquitinating enzyme in the parasite G.intestinalis.application/pdfspaUniversidad Nacional de Colombia - Sede Bogotá - Facultad de Ciencias - Departamento de Químicahttps://revistas.unal.edu.co/index.php/rcolquim/article/view/53445Universidad Nacional de Colombia Revistas electrónicas UN Revista Colombiana de QuímicaRevista Colombiana de QuímicaAlvarado, Magda E and González, Camila A and Wasserman, Moisés and Rubiano, Claudia C (2014) Preliminary study of the enzyme ubiquitin carboxylterminal hydrolase 14 (UBP6) in Giardia intestinalis: structural bioinformatic analysis and transcriptional profile during encystation. Revista Colombiana de Química, 43 (2). pp. 32-40. ISSN 2357-379154 Química y ciencias afines / Chemistrydeubiquitinating enzymesubiquitinGiardia intestinalisencystationPreliminary study of the enzyme ubiquitin carboxylterminal hydrolase 14 (UBP6) in Giardia intestinalis: structural bioinformatic analysis and transcriptional profile during encystationArtículo de revistainfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_2df8fbb1http://purl.org/coar/version/c_970fb48d4fbd8a85Texthttp://purl.org/redcol/resource_type/ARTORIGINAL53445-262538-1-SM.pdfapplication/pdf2972565https://repositorio.unal.edu.co/bitstream/unal/66323/1/53445-262538-1-SM.pdfe40fe1f7260e09ac93fa79b8797215f1MD51THUMBNAIL53445-262538-1-SM.pdf.jpg53445-262538-1-SM.pdf.jpgGenerated Thumbnailimage/jpeg9397https://repositorio.unal.edu.co/bitstream/unal/66323/2/53445-262538-1-SM.pdf.jpgb036e00c5e71219f6e4f390044c17003MD52unal/66323oai:repositorio.unal.edu.co:unal/663232024-05-15 23:09:21.537Repositorio Institucional Universidad Nacional de Colombiarepositorio_nal@unal.edu.co
dc.title.spa.fl_str_mv Preliminary study of the enzyme ubiquitin carboxylterminal hydrolase 14 (UBP6) in Giardia intestinalis: structural bioinformatic analysis and transcriptional profile during encystation
title Preliminary study of the enzyme ubiquitin carboxylterminal hydrolase 14 (UBP6) in Giardia intestinalis: structural bioinformatic analysis and transcriptional profile during encystation
spellingShingle Preliminary study of the enzyme ubiquitin carboxylterminal hydrolase 14 (UBP6) in Giardia intestinalis: structural bioinformatic analysis and transcriptional profile during encystation
54 Química y ciencias afines / Chemistry
deubiquitinating enzymes
ubiquitin
Giardia intestinalis
encystation
title_short Preliminary study of the enzyme ubiquitin carboxylterminal hydrolase 14 (UBP6) in Giardia intestinalis: structural bioinformatic analysis and transcriptional profile during encystation
title_full Preliminary study of the enzyme ubiquitin carboxylterminal hydrolase 14 (UBP6) in Giardia intestinalis: structural bioinformatic analysis and transcriptional profile during encystation
title_fullStr Preliminary study of the enzyme ubiquitin carboxylterminal hydrolase 14 (UBP6) in Giardia intestinalis: structural bioinformatic analysis and transcriptional profile during encystation
title_full_unstemmed Preliminary study of the enzyme ubiquitin carboxylterminal hydrolase 14 (UBP6) in Giardia intestinalis: structural bioinformatic analysis and transcriptional profile during encystation
title_sort Preliminary study of the enzyme ubiquitin carboxylterminal hydrolase 14 (UBP6) in Giardia intestinalis: structural bioinformatic analysis and transcriptional profile during encystation
dc.creator.fl_str_mv Alvarado, Magda E
González, Camila A
Wasserman, Moisés
Rubiano, Claudia C
dc.contributor.author.spa.fl_str_mv Alvarado, Magda E
González, Camila A
Wasserman, Moisés
Rubiano, Claudia C
dc.subject.ddc.spa.fl_str_mv 54 Química y ciencias afines / Chemistry
topic 54 Química y ciencias afines / Chemistry
deubiquitinating enzymes
ubiquitin
Giardia intestinalis
encystation
dc.subject.proposal.spa.fl_str_mv deubiquitinating enzymes
ubiquitin
Giardia intestinalis
encystation
description This paper presents a combined approachwith two aims. The first is to analyze thereported sequence of the enzyme ubiquitincarboxyl-terminal hydrolase 14 of Giardiaintestinalis (UBP6) through computationalmethods to find components related withits hypothetical function. The second isto determine if the protein-coding gene isexpressed in G. intestinalis and, if such isthe case, also determine its transcriptionpattern along the life cycle of the parasite. Itwas established that the protein belongs tothe family of Cys-dependent deubiquitinasesand more specifically to ubiquitin specificproteases (USPs). Moreover, the catalyticcenter with the complete triad as well astypical features of the USP motif were alsoidentified. Since the computational findingssuggest that the enzyme could be functional,reverse transcription coupled to PCR wasused as a first approach to establish if in factthe coding gene is expressed in the parasite.Interestingly, it was found not only thatthe gene is expressed, but also that thereis a transcription variation along the lifecycle of the parasite. These two findings arethe starting point for further studies sincethey tentatively suggest that this enzymecould be involved in the protein turnoverthat occurs during parasite encystation.Although preliminary, this study is the firstreport concerning the study of a specificdeubiquitinating enzyme in the parasite G.intestinalis.
publishDate 2014
dc.date.issued.spa.fl_str_mv 2014-05-01
dc.date.accessioned.spa.fl_str_mv 2019-07-03T01:54:32Z
dc.date.available.spa.fl_str_mv 2019-07-03T01:54:32Z
dc.type.spa.fl_str_mv Artículo de revista
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dc.identifier.issn.spa.fl_str_mv ISSN: 2357-3791
dc.identifier.uri.none.fl_str_mv https://repositorio.unal.edu.co/handle/unal/66323
dc.identifier.eprints.spa.fl_str_mv http://bdigital.unal.edu.co/67347/
identifier_str_mv ISSN: 2357-3791
url https://repositorio.unal.edu.co/handle/unal/66323
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dc.language.iso.spa.fl_str_mv spa
language spa
dc.relation.spa.fl_str_mv https://revistas.unal.edu.co/index.php/rcolquim/article/view/53445
dc.relation.ispartof.spa.fl_str_mv Universidad Nacional de Colombia Revistas electrónicas UN Revista Colombiana de Química
Revista Colombiana de Química
dc.relation.references.spa.fl_str_mv Alvarado, Magda E and González, Camila A and Wasserman, Moisés and Rubiano, Claudia C (2014) Preliminary study of the enzyme ubiquitin carboxylterminal hydrolase 14 (UBP6) in Giardia intestinalis: structural bioinformatic analysis and transcriptional profile during encystation. Revista Colombiana de Química, 43 (2). pp. 32-40. ISSN 2357-3791
dc.rights.spa.fl_str_mv Derechos reservados - Universidad Nacional de Colombia
dc.rights.coar.fl_str_mv http://purl.org/coar/access_right/c_abf2
dc.rights.license.spa.fl_str_mv Atribución-NoComercial 4.0 Internacional
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dc.rights.accessrights.spa.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv Atribución-NoComercial 4.0 Internacional
Derechos reservados - Universidad Nacional de Colombia
http://creativecommons.org/licenses/by-nc/4.0/
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
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dc.publisher.spa.fl_str_mv Universidad Nacional de Colombia - Sede Bogotá - Facultad de Ciencias - Departamento de Química
institution Universidad Nacional de Colombia
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