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dc.contributor.author Giordana, Lucila
dc.contributor.author Suárez Mantilla, Brian
dc.contributor.author Santana, Marianela
dc.contributor.author Silber, Ariel Mariano
dc.contributor.author Nowicki, Cristina
dc.date.available 2018-01-04T14:26:25Z
dc.date.issued 2014-03
dc.identifier.citation Nowicki, Cristina; Silber, Ariel Mariano; Santana, Marianela; Suárez Mantilla, Brian; Giordana, Lucila; Cystathionine γ-lyase, an Enzyme Related to the Reverse Transsulfuration Pathway, is Functional in Leishmania spp.; Wiley Blackwell Publishing, Inc; Journal of Eukaryotic Microbiology; 61; 2; 3-2014; 204-213
dc.identifier.issn 1066-5234
dc.identifier.uri http://hdl.handle.net/11336/32287
dc.description.abstract Leishmania parasites seem capable of producing cysteine by de novo biosynthesis, similarly to bacteria, some pathogenic protists, and plants. In Leishmania spp., cysteine synthase (CS) and cystathionine β-synthase (CBS) are expected to participate in this metabolic process. Moreover, the reverse transsulfuration pathway (RTP) is also predicted to be operative in this trypanosomatid because CBS also catalyzes the condensation of serine with homocysteine, and a gene encoding a putative cystathionine γ-lyase (CGL) is present in all the sequenced genomes. Our results show that indeed, Leishmania major CGL is able to rescue the wild-type phenotype of a Saccharomyces cerevisiae CGL-null mutant and is susceptible to inhibition by an irreversible CGL inhibitor, DL-propargylglycine (PAG). In Leishmania promastigotes, CGL and CS are cytosolic enzymes. The coexistence of de novo synthesis with the RTP is extremely rare in most living organisms; however, despite this potentially high redundancy in cysteine production, PAG arrests the proliferation of L. major promastigotes with an IC50 of approximately 65 μM. These findings raise new questions regarding the biological role of CGL in these pathogens and indicate the need for understanding the molecular mechanism of PAG action in vivo to identify the potential targets affected by this drug.
dc.format application/pdf
dc.language.iso eng
dc.publisher Wiley Blackwell Publishing, Inc
dc.rights info:eu-repo/semantics/restrictedAccess
dc.rights.uri https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject Leishmania parasites
dc.subject DL-propargylglycine
dc.subject.classification Otras Ciencias Biológicas
dc.subject.classification Ciencias Biológicas
dc.subject.classification CIENCIAS NATURALES Y EXACTAS
dc.title Cystathionine γ-lyase, an Enzyme Related to the Reverse Transsulfuration Pathway, is Functional in Leishmania spp.
dc.type info:eu-repo/semantics/article
dc.type info:ar-repo/semantics/artículo
dc.type info:eu-repo/semantics/publishedVersion
dc.date.updated 2018-01-03T19:05:22Z
dc.journal.volume 61
dc.journal.number 2
dc.journal.pagination 204-213
dc.journal.pais Reino Unido
dc.journal.ciudad Londres
dc.description.fil Fil: Giordana, Lucila. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
dc.description.fil Fil: Suárez Mantilla, Brian. Universidade de Sao Paulo; Brasil
dc.description.fil Fil: Santana, Marianela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
dc.description.fil Fil: Silber, Ariel Mariano. Universidade de Sao Paulo; Brasil
dc.description.fil Fil: Nowicki, Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
dc.journal.title Journal of Eukaryotic Microbiology
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/jeu.12100/abstract
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1111/jeu.12100
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info:eu-repo/semantics/restrictedAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)