ArticleNucleic acids research2013
Cooperative recruitment of HMGB1 during V(D)J recombination through interactions with RAG1 and DNA.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 52 citations in OpenAlex.
- Proximity-based proteomic profiling uncovers distinct interactome of human RAG1 and RAG2.Acta biochimica et biophysica Sinica · 2026Article
- Structures reveal how the Cas1-2/3 integrase captures, delivers, and integrates foreign DNA into CRISPR loci.Structure (London, England : 1993) · 2025Article
- HMGB1 couples LEF1 to regulate B cell immunity.JCI insight · 2025Article
- Multiple reaction monitoring assays for large-scale quantitation of proteins from 20 mouse organs and tissues.Communications biology · 2024Article
- Structure reveals why genome folding is necessary for site-specific integration of foreign DNA into CRISPR arrays.Nature structural & molecular biology · 2023Article
- Role of the mechanisms for antibody repertoire diversification in monoclonal light chain deposition disorders: when a friend becomes foe.Frontiers in immunology · 2023Review
- Nonamer dependent RAG cleavage at CpGs can explain mechanism of chromosomal translocations associated to lymphoid cancers.PLoS genetics · 2022Article
- Targeting HMGB1: An available Therapeutic Strategy for Breast Cancer Therapy.International journal of biological sciences · 2022Review
- The extracellular innate-immune effector HMGB1 limits pathogenic bacterial biofilm proliferation.The Journal of clinical investigation · 2021Article
- HMGB1 coordinates SASP-related chromatin folding and RNA homeostasis on the path to senescence.Molecular systems biology · 2021Article
- Functional Diversity of Non-Histone Chromosomal Protein HmgB1.International journal of molecular sciences · 2020Review
- Interactions of high mobility group box protein 1 (HMGB1) with nucleic acids: Implications in DNA repair and immune responses.DNA repair · 2019Review
- Below the surface: The inner lives of TLR4 and TLR9.Journal of leukocyte biology · 2019Review
- A novelBlood · 2019Article
- HMGB1 contributes to the irradiation-induced endothelial barrier injury through receptor for advanced glycation endproducts (RAGE).Journal of cellular physiology · 2018Article
- HMGB1 induces lung fibroblast to myofibroblast differentiation through NF‑κB‑mediated TGF‑β1 release.Molecular medicine reports · 2017Article
- Tools to Study the Role of Architectural Protein HMGB1 in the Processing of Helix Distorting, Site-specific DNA Interstrand Crosslinks.Journal of visualized experiments : JoVE · 2016Article
- High mobility group protein 1: A collaborator in nucleosome dynamics and estrogen-responsive gene expression.World journal of biological chemistry · 2016Review
- Mechanisms of DNA Transposition.Microbiology spectrum · 2015Review
- The architecture of the 12RSS in V(D)J recombination signal and synaptic complexes.Nucleic acids research · 2015Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
During V(D)J recombination, recombination activating gene (RAG)1 and RAG2 bind and cleave recombination signal sequences (RSSs), aided by the ubiquitous DNA-binding/-bending proteins high-mobility group box protein (HMGB)1 or HMGB2. HMGB1/2 play a critical, although poorly understood, role in vitro in the assembly of functional RAG-RSS complexes, into which HMGB1/2 stably incorporate. The mechanism of HMGB1/2 recruitment is unknown, although an interaction with RAG1 has been suggested. Here, we report data demonstrating only a weak HMGB1-RAG1 interaction in the absence of DNA in several assays, including fluorescence anisotropy experiments using a novel Alexa488-labeled HMGB1 protein. Addition of DNA to RAG1 and HMGB1 in fluorescence anisotropy experiments, however, results in a substantial increase in complex formation, indicating a synergistic binding effect. Pulldown experiments confirmed these results, as HMGB1 was recruited to a RAG1-DNA complex in a RAG1 concentration-dependent manner and, interestingly, without strict RSS sequence specificity. Our finding that HMGB1 binds more tightly to a RAG1-DNA complex over RAG1 or DNA alone provides an explanation for the stable integration of this typically transient architectural protein in the V(D)J recombinase complex throughout recombination. These findings also have implications for the order of events during RAG-DNA complex assembly and for the stabilization of sequence-specific and non-specific RAG1-DNA interactions.
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Registered trials
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