Human Rad50 Is Physically Associated with Human Mre11: Identification of a Conserved Multiprotein Complex Implicated in Recombinational DNA Repair

Dolganov, Gregory M.; Maser, Richard S.; Novikov, Alexander; Tosto, Liana; Chong, Susan; Bressan, Debra A.; Petrini, John H. J.

doi:10.1128/mcb.16.9.4832

Cited by 224DNA Repair MechanismsFungal and yeast genetics researchGenomics and Chromatin Dynamics

Human Rad50 Is Physically Associated with Human Mre11: Identification of a Conserved Multiprotein Complex Implicated in Recombinational DNA Repair

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Dolganov, Gregory M., Maser, Richard S., Novikov, Alexander, Tosto, Liana, Chong, Susan, Bressan, Debra A., Petrini, John H. J.·1996·Molecular and Cellular Biology

DOI 10.1128/mcb.16.9.4832PMC PMC231485

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Abstract

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.
“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]
The hRad50 protein complexes section reports a stable association between human Mre11 and Rad50. The passages do not report binding between Mre11 and Nbs1, so this source supports only the Rad50 part of the claim. (LLM, conf=0.90)
Experimental — accuracy not yet measured
A multimeric complex, including Mre11, Nbs1, Rad50, and other proteins, is necessary to repair broken DNA.
“Therefore, a multimeric complex, including Mre11, Nbs1, Rad50, and other proteins, is necessary to repair broken DNA.”
From Mdm2 Binds to Nbs1 at Sites of DNA Damage and Regulates Double Strand Break Repair (2005) · cites this paper as [3]
The Discussion (page unavailable in our copy) reports a stable human Mre11–Rad50 complex associated with three other proteins and implicates it in double-strand-break repair. It does not identify Nbs1: the authors only speculate that a 95-kDa protein is a human Xrs2 homolog. The paper also does not establish that the full complex is necessary for repair. (LLM, conf=0.88)
Experimental — accuracy not yet measured

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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
DOI: 10.1128/mcb.16.9.4832
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
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
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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Human Rad50 Is Physically Associated with Human Mre11: Identification of a Conserved Multiprotein Complex Implicated in Recombinational DNA Repair

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