Biochemical and structural characterization of the RT domain of Leishmania sp. telomerase reverse transcriptase

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorSorbonne Université-
Autor(es): dc.creatorda Silva, Vitor Luiz-
Autor(es): dc.creatorde Paiva, Stephany Cacete-
Autor(es): dc.creatorde Oliveira, Hamine Cristina-
Autor(es): dc.creatorFernandes, Carlos Alexandre H.-
Autor(es): dc.creatorSalvador, Guilherme Henrique Marchi-
Autor(es): dc.creatorFontes, Marcos Roberto de M.-
Autor(es): dc.creatorCano, Maria Isabel N.-
Data de aceite: dc.date.accessioned2025-08-21T15:39:26Z-
Data de disponibilização: dc.date.available2025-08-21T15:39:26Z-
Data de envio: dc.date.issued2025-04-29-
Data de envio: dc.date.issued2023-10-31-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.bbagen.2023.130451-
Fonte completa do material: dc.identifierhttps://hdl.handle.net/11449/304416-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/304416-
Descrição: dc.descriptionBackground: The Leishmania genus comprises parasites that cause leishmaniasis, a neglected disease spread worldwide. Leishmania sp. telomeres are composed of TTAGGG repeats maintained by telomerase. In most eukaryotes, the enzyme minimal complex contains the TER (telomerase RNA) and the TERT (telomerase reverse transcriptase) components. The TERT holds the enzyme catalytic core and is formed by four structural and functional domains (TEN, Telomerase Essential N-terminal; TRBD, Telomerase RNA Binding Domain; RT, the reverse transcriptase domain and CTE, C-Terminal Extension domain). Methods and results: Amino acid sequence alignments, protein structure prediction analysis, and protein: nucleic acid interaction assays were used to show that the Leishmania major RT domain preserves the canonical structural elements found in higher eukaryotes, including the canonical motifs and the aspartic acid residues that stabilize the Mg2+ ion cofactor. Furthermore, amino acid substitutions specific to the Leishmania genus and partial conservation of the residues involved with nucleic acid interactions are shown. The purified recombinant Leishmania RT protein is biochemically active and interacts with the G-rich telomeric strand and the TER template sequence. Conclusion: Our results highlight that the telomerase catalysis mechanism is conserved in a pathogen of medical importance despite the structural peculiarities present in the parasite's RT domain.-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionDepartment of Chemical and Biological Sciences Institute of Biosciences São Paulo State University (UNESP), SP-
Descrição: dc.descriptionDepartment of Biophysics and Pharmacology Institute of Biosciences São Paulo State University (UNESP), SP-
Descrição: dc.descriptionUMR 7590 CNRS Muséum National d'Histoire Naturelle IRD Institut de Minéralogie Physique des Matériaux et de Cosmochimie IMPMC Sorbonne Université-
Descrição: dc.descriptionInstitute for Advanced Studies of the Sea (IEAMAR) São Paulo State University (UNESP), SP-
Descrição: dc.descriptionDepartment of Chemical and Biological Sciences Institute of Biosciences São Paulo State University (UNESP), SP-
Descrição: dc.descriptionDepartment of Biophysics and Pharmacology Institute of Biosciences São Paulo State University (UNESP), SP-
Descrição: dc.descriptionInstitute for Advanced Studies of the Sea (IEAMAR) São Paulo State University (UNESP), SP-
Descrição: dc.descriptionCNPq: 150448/2022-8-
Descrição: dc.descriptionFAPESP: 2019/05239-8-
Descrição: dc.descriptionFAPESP: 2021/14798-0-
Descrição: dc.descriptionFAPESP: MINC 2018/04375-2-
Descrição: dc.descriptionCNPq: MINC 302433/2019-8-
Descrição: dc.descriptionFAPESP: MRFM 2019/05958-4-
Descrição: dc.descriptionCNPq: MRFM 302643/2021-4-
Idioma: dc.languageen-
Relação: dc.relationBiochimica et Biophysica Acta - General Subjects-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectLeishmania-
Palavras-chave: dc.subjectProtein: Nucleic acid interactions-
Palavras-chave: dc.subjectRecombinant protein purification-
Palavras-chave: dc.subjectRT domain-
Palavras-chave: dc.subjectStructure prediction-
Título: dc.titleBiochemical and structural characterization of the RT domain of Leishmania sp. telomerase reverse transcriptase-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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