Cited by 111Mitochondrial Function and PathologyCell death mechanisms and regulationDNA Repair Mechanisms

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Generation and Characterization of Endonuclease G Null Mice

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Irvine, Ryan A., Adachi, Noritaka, Shibata, Darryl K., Cassell, Geoffrey D., Yu, Kefei, Karanjawala, Zarir E., Hsieh, Chih-Lin, Lieber, Michael R.·2005·Molecular and Cellular Biology

DOI 10.1128/mcb.25.1.294-302.2005PMC PMC538798

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Abstract

Endonuclease G (endo G) is one of the most abundant nucleases in eukaryotic cells. It is encoded in the nucleus and imported to the mitochondrial intermembrane space. This nuclease is active on single- and double-stranded DNA. We genetically disrupted the endo G gene in mice without disturbing a conserved, overlapping gene of unknown function that is oriented tail to tail with the endo G gene. In these mice, the production of endo G protein is not detected, and the disruption abolishes the nuclease activity of endo G. The absence of endo G has no effect on mitochondrial DNA copy number, structure, or mutation rate over the first five generations. There is also no obvious effect on nuclear DNA degradation in standard apoptosis assays. The endo G null mice are viable and show no age-related or generational abnormalities anatomically or histologically. We infer that this highly conserved protein has no mitochondrial or apoptosis function that can discerned by the assays described here and that it may have a function yet to be determined. The early embryonic lethality of endo G null mice recently reported by others may be due to the disruption of the gene that overlaps the endo G gene.

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Endonuclease G is an apoptotic DNase when released from mitochondria
Li, L. Y., Luo, X., & Wang, X. (2001) · Nature · doi:10.1038/35083620 · Cited by 1,787
Sequence and gene organization of mouse mitochondrial DNA.
Bibb, M., Etten, R. V., Wright, C. T., Walberg, M. W., & Clayton, D. A. (1981) · Cell · doi:10.1016/0092-8674(81)90300-7 · Cited by 1,619
R-loops at immunoglobulin class switch regions in the chromosomes of stimulated B cells
Yu, K.-F., Chédin, F., Hsieh, C.-L., Wilson, T. E., & Lieber, M. (2003) · Nature Immunology · doi:10.1038/ni919 · Cited by 767
Self-citation
Replication And Transcription Of Vertebrate Mitochondrial Dna
Clayton, D. A. (1991) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.07.110191.002321 · Cited by 652
An abundance of bidirectional promoters in the human genome.Preprint
Trinklein, N., Aldred, S. F., Hartman, S. J., Schroeder, D. I., Otillar, R., & Myers, R. (2003) · Genome Research · doi:10.1101/gr.1982804 · Cited by 641
The harlequin mouse mutation downregulates apoptosis-inducing factor
Klein, J. A., Longo-Guess, C. M., Rossmann, M. P., Seburn, K. L., Hurd, R. E., Frankel, W. N., Bronson, R. T., & Ackerman, S. L. (2002) · Nature · doi:10.1038/nature01034 · Cited by 605
Mitochondrial endonuclease G is important for apoptosis in C. elegans
Parrish, J., Li, L., Klotz, K., Ledwich, D., Wang, X., & Xue, D. (2001) · Nature · doi:10.1038/35083608 · Cited by 427
Transcription and Replication of Animal Mitochondrial DNAs
Clayton, D. A. (1992) · International review of cytology · doi:10.1016/s0074-7696(08)62067-7 · Cited by 360
Failure to produce mitochondrial DNA results in embryonic lethality in Rnaseh1 null mice
Cerritelli, S. M., Frolova, E. G., Feng, C., Grinberg, A., Love, P. E., & Crouch, R. J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00088-1 · Cited by 358
Bidirectional Gene Organization
Adachi, N., & Lieber, M. R. (2002) · Cell · doi:10.1016/s0092-8674(02)00758-4 · Cited by 346
Self-citation

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Gupta, S., Kass, G. E. N., Szegezdi, É., & Joseph, B. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00697.x · Cited by 283
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Dissociating the dual roles of apoptosis‐inducing factor in maintaining mitochondrial structure and apoptosis
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He, B., Lü, N., & Zhou, Z. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.08.008 · Cited by 131
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Prokhorova, E. A., Zamaraev, A. V., Kopeina, G. S., Zhivotovsky, B., & Lavrik, I. N. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2031-y · Cited by 116
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David, K. K., Sasaki, M., Yu, S.-W., Dawson, T. M., & Dawson, V. L. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401787 · Cited by 96
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Kagan, R. M., & Reid, W. J. (1986) · PubMed · Cited by 49
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Wang, X., Marina, V., & Alexei, G. (2011) · InTech eBooks · doi:10.5772/25585 · Cited by 1
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Yang, N., & Goping, I. S. (2013) · Colloquium Series on Building Blocks of the Cell Cell Structure and Function · doi:10.4199/c00080ed1v01y201303bbc003 · Cited by 1
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Xie, X., Li, J., Zhang, X., Mo, S., Li, A., Sun, T., Xie, F.-Y., Luo, S., Wang, G., Ou, X., et al. (2024) · Biology Open · doi:10.1242/bio.061730 · Cited by 1
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Fatokun, A. A. (2012) · TSpace (University of Toronto) · Cited by 1
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Misic, V. (2013) · Brock University Digital Repository (Brock University) · Cited by 1
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Ye, J. (2012) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)

Authors: Irvine, R. A., Adachi, N., Shibata, D. K., Cassell, G. D., Yu, K., Karanjawala, Z. E., Hsieh, C.-L., & Lieber, M. R.
Affiliations: University of Southern California (US)
Departments of Pathology, of Biochemistry & Molecular Biology, of Molecular Microbiology & Immunology, and of Biological Sciences
Corresponding author: Lieber, Michael R.
ORCID: Adachi, Noritaka
Shibata, Darryl K.
Yu, Kefei
Hsieh, Chih-Lin
Lieber, Michael R.
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 2005-01
Volume: 25
Issue: 1
Pages: 294-302
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.25.1.294-302.2005
PMC: PMC538798
OpenAlex: W2125483893
Cited by: 111
References: 30
Citations by year: 2026: 2 · 2025: 1 · 2024: 3 · 2023: 4 · 2022: 1 · 2021: 4 · 2020: 2 · 2019: 1 · 2018: 2 · 2017: 1 · 2016: 5 · 2015: 3 · 2014: 2 · 2013: 7 · 2012: 6
FWCI: 3.67
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of General Medical Sciences (R01GM056984)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Keywords: endonuclease G, gene knockout, mitochondrial DNA, mitochondrial intermembrane space, nuclease activity, mitochondrial DNA copy number, apoptosis, nuclear DNA degradation, embryonic lethality
MeSH terms: Animals, Cell Nucleus, Cell Survival, Chromatin, DNA, DNA, Mitochondrial, Endodeoxyribonucleases, Enzyme-Linked Immunosorbent Assay, Immunoglobulin G, Immunoglobulin M, Mice, Inbred C57BL, Mice, Mutant Strains, Mice, Transgenic, Mitochondria, Models, Genetic, Mutation, Plasmids, Spleen, Blotting, Southern, Blotting, Western, Apoptosis, Transgenes, Mice, DNA Fragmentation

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Generation and Characterization of Endonuclease G Null Mice

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