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Human Rad50 Is Physically Associated with Human Mre11: Identification of a Conserved Multiprotein Complex Implicated in Recombinational DNA Repair
Open accessAbstract
In this report, we describe the identification and molecular characterization of a human RAD50 homolog, hRAD50. hRAD50 was included in a collection of cDNAs which were isolated by a direct cDNA selection strategy focused on the chromosomal interval spanning 5q23 to 5q31. Alterations of the 5q23-q31 interval are frequently observed in myelodysplasia and myeloid leukemia. This strategy was thus undertaken to create a detailed genetic map of that region. Saccharomyces cerevisiae RAD50 (ScRAD50) is one of three yeast RAD52 epistasis group members (ScRAD50, ScMRE11, and ScXRS2) in which mutations eliminate meiotic recombination but confer a hyperrecombinational phenotype in mitotic cells. The yeast Rad50, Mre11, and Xrs2 proteins appear to act in a multiprotein complex, consistent with the observation that the corresponding mutants confer essentially identical phenotypes. In this report, we demonstrate that the human Rad50 and Mre11 proteins are stably associated in a protein complex which may include three other proteins. hRAD50 is expressed in all tissues examined, but mRNA levels are significantly higher in the testis. Other human RAD52 epistasis group homologs exhibit this expression pattern, suggesting the involvement of human RAD52 epistasis group proteins in meiotic recombination. Human RAD52 epistasis group proteins are highly conserved and act in protein complexes that are analogous to those of their yeast counterparts. These findings indicate that the function of the RAD52 epistasis group is conserved in human cells.
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“Mre11 binds both Nbs1 and Rad50 (3,4).”
From Mdm2 Binds to Nbs1 at Sites of DNA Damage and Regulates Double Strand Break Repair (2005) · cites this paper as [3]
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“Therefore, a multimeric complex, including Mre11, Nbs1, Rad50, and other proteins, is necessary to repair broken DNA.”
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Metadata
- Authors
- Dolganov, G. M., Maser, R. S., Novikov, A., Tosto, L., Chong, S., Bressan, D. A., & Petrini, J. H. J.
- Affiliations
- Human Genome Group, Genelabs Technologies, Inc., Redwood City, California 94063
- University of Wisconsin–Madison (US)
- ORCID
- Petrini, John H. J.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 1996-09-01
- Volume
- 16
- Issue
- 9
- Pages
- 4832-4841
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC231485
- OpenAlex
- W1794569271
- Cited by
- 224
- References
- 85
- Citations by year
- 2026: 1 · 2025: 4 · 2023: 2 · 2022: 1 · 2021: 1 · 2020: 1 · 2019: 4 · 2017: 3 · 2016: 2 · 2015: 5 · 2014: 3 · 2013: 2 · 2012: 3
- FWCI
- 7.95
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular and Cellular Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health
- National Institute of General Medical Sciences (5T32GM07133, T32GM007133)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- RAD50, MRE11, RAD52 epistasis group, recombinational DNA repair, protein complexes, meiotic recombination, myelodysplastic syndrome, myeloid leukemia, Saccharomyces cerevisiae, Xrs2, testis expression, functional conservation
- MeSH terms
- Amino Acid Sequence, Base Sequence, Chromosomes, Human, Pair 5, DNA Repair, DNA-Binding Proteins, Endodeoxyribonucleases, Exodeoxyribonucleases, Female, Fibroblasts, Fungal Proteins, Humans, Leukemia, Myeloid, Liver, Male, Molecular Sequence Data, Ovary, Recombination, Genetic, RNA, Messenger, Saccharomyces cerevisiae, Testis, Thymus Gland, Sequence Alignment, Sequence Homology, Amino Acid, DNA, Complementary, Saccharomyces cerevisiae Proteins, Macromolecular Substances, Multiprotein Complexes, Rad52 DNA Repair and Recombination Protein
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