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Leishmania infantum EndoG is an endo/exo-nuclease essential for parasite survival.

作者信息

Rico Eva, Oliva Cristina, Gutierrez Kilian Jesús, Alzate Juan Fernando, Genes Carlos Mario, Moreno David, Casanova Elena, Gigante Alba, Pérez-Pérez María-Jesús, Camarasa María-José, Clos Joachim, Gago Federico, Jiménez-Ruiz Antonio

机构信息

Departamento de Biología de Sistemas-Unidad Asociada al Consejo Superior de Investigaciones Científicas (CSIC), Universidad de Alcalá, Alcalá de Henares, Madrid, Spain.

Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad de Antioquia, Medellín, Colombia.

出版信息

PLoS One. 2014 Feb 26;9(2):e89526. doi: 10.1371/journal.pone.0089526. eCollection 2014.

DOI:10.1371/journal.pone.0089526
PMID:24651293
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3971528/
Abstract

EndoG, a member of the DNA/RNA non-specific ββα-metal family of nucleases, has been demonstrated to be present in many organisms, including Trypanosomatids. This nuclease participates in the apoptotic program in these parasites by migrating from the mitochondrion to the nucleus, where it takes part in the degradation of genomic DNA that characterizes this process. We now demonstrate that Leishmania infantum EndoG (LiEndoG) is an endo-exonuclease that has a preferential 5' exonuclease activity on linear DNA. Regardless of its role during apoptotic cell death, this enzyme seems to be necessary during normal development of the parasites as indicated by the reduced growth rates observed in LiEndoG hemi-knockouts and their poor infectivity in differentiated THP-1 cells. The pro-life role of this protein is also corroborated by the higher survival rates of parasites that over-express this protein after treatment with the LiEndoG inhibitor Lei49. Taken together, our results demonstrate that this enzyme plays essential roles in both survival and death of Leishmania parasites.

摘要
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f38/3971528/ce49b9bcfa2f/pone.0089526.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f38/3971528/a56733d19e23/pone.0089526.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f38/3971528/e2e6946c308a/pone.0089526.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f38/3971528/f91b66fc4ce3/pone.0089526.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f38/3971528/d03c58409b39/pone.0089526.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f38/3971528/8444358fd34e/pone.0089526.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f38/3971528/ce49b9bcfa2f/pone.0089526.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f38/3971528/a56733d19e23/pone.0089526.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f38/3971528/e2e6946c308a/pone.0089526.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f38/3971528/f91b66fc4ce3/pone.0089526.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f38/3971528/d03c58409b39/pone.0089526.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f38/3971528/8444358fd34e/pone.0089526.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f38/3971528/ce49b9bcfa2f/pone.0089526.g006.jpg

相似文献

[1]
Leishmania infantum EndoG is an endo/exo-nuclease essential for parasite survival.

PLoS One. 2014-2-26

[2]
Leishmania infantum expresses a mitochondrial nuclease homologous to EndoG that migrates to the nucleus in response to an apoptotic stimulus.

Mol Biochem Parasitol. 2009-1

[3]
Structure-based domain assignment in Leishmania infantum EndoG: characterization of a pH-dependent regulatory switch and a C-terminal extension that largely dictates DNA substrate preferences.

Nucleic Acids Res. 2017-9-6

[4]
EXOG, a novel paralog of Endonuclease G in higher eukaryotes.

Nucleic Acids Res. 2008-3

[5]
Meiotic viral attenuation through an ancestral apoptotic pathway.

Proc Natl Acad Sci U S A. 2019-7-2

[6]
Conservation of the pro-apoptotic nuclease activity of endonuclease G in unicellular trypanosomatid parasites.

J Cell Sci. 2008-1-1

[7]
5'-Trityl-substituted thymidine derivatives as a novel class of antileishmanial agents: Leishmania infantum EndoG as a potential target.

ChemMedChem. 2013-4-26

[8]
A domain in human EXOG converts apoptotic endonuclease to DNA-repair exonuclease.

Nat Commun. 2017-5-3

[9]
Structural and functional characterization of mitochondrial EndoG, a sugar non-specific nuclease which plays an important role during apoptosis.

J Mol Biol. 2004-4-23

[10]
Mitochondrial redox metabolism in trypanosomatids is independent of tryparedoxin activity.

PLoS One. 2010-9-8

引用本文的文献

[1]
An inclusive assessment of apoptosis mechanisms in species: A narrative literature review.

Curr Res Parasitol Vector Borne Dis. 2025-4-17

[2]
Cell death in Leishmania.

Parasite. 2019-12-11

[3]
Structure-based domain assignment in Leishmania infantum EndoG: characterization of a pH-dependent regulatory switch and a C-terminal extension that largely dictates DNA substrate preferences.

Nucleic Acids Res. 2017-9-6

本文引用的文献

[1]
5'-Trityl-substituted thymidine derivatives as a novel class of antileishmanial agents: Leishmania infantum EndoG as a potential target.

ChemMedChem. 2013-4-26

[2]
Selenocyanates and diselenides: a new class of potent antileishmanial agents.

Eur J Med Chem. 2011-4-28

[3]
Crystal structure of the EndoG/EndoGI complex: mechanism of EndoG inhibition.

Nucleic Acids Res. 2009-11

[4]
Leishmania infantum expresses a mitochondrial nuclease homologous to EndoG that migrates to the nucleus in response to an apoptotic stimulus.

Mol Biochem Parasitol. 2009-1

[5]
The caspase-independent algorithm of programmed cell death in Leishmania induced by baicalein: the role of LdEndoG, LdFEN-1 and LdTatD as a DNA 'degradesome'.

Cell Death Differ. 2008-10

[6]
Production of monoclonal antibodies.

Curr Protoc Immunol. 2006-9

[7]
EXOG, a novel paralog of Endonuclease G in higher eukaryotes.

Nucleic Acids Res. 2008-3

[8]
Conservation of the pro-apoptotic nuclease activity of endonuclease G in unicellular trypanosomatid parasites.

J Cell Sci. 2008-1-1

[9]
Endonuclease G regulates budding yeast life and death.

Mol Cell. 2007-1-26

[10]
Heat-induced programmed cell death in Leishmania infantum is reverted by Bcl-X(L) expression.

Apoptosis. 2006-2

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