ArticleMolecular and cellular biology2005
Determinants of HMGB proteins required to promote RAG1/2-recombination signal sequence complex assembly and catalysis during V(D)J recombination.
Article in Molecular and cellular biology, 2005. 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, 47 citations in OpenAlex.
- The nonamer code for RAG-mediated recombination in vivo.Nucleic acids research · 2025Article
- HMGB1 couples LEF1 to regulate B cell immunity.JCI insight · 2025Article
- The HMGB chromatin protein Nhp6A can bypass obstacles when traveling on DNA.Nucleic acids research · 2020Article
- HIV‑1 integrase inhibitors targeting various DDE transposases: Retroviral integration versus RAG‑mediated recombination (Review).Molecular medicine reports · 2019Review
- Interactions of high mobility group box protein 1 (HMGB1) with nucleic acids: Implications in DNA repair and immune responses.DNA repair · 2019Review
- HMGB1 contributes to the irradiation-induced endothelial barrier injury through receptor for advanced glycation endproducts (RAGE).Journal of cellular physiology · 2018Article
- Unconventional Pathways of Secretion Contribute to Inflammation.International journal of molecular sciences · 2017Review
- High mobility group protein 1: A collaborator in nucleosome dynamics and estrogen-responsive gene expression.World journal of biological chemistry · 2016Review
- HMGB1 in health and disease.Molecular aspects of medicine · 2014Review
- Synapsis alters RAG-mediated nicking at Tcrb recombination signal sequences: implications for the “beyond 12/23” rule.Molecular and cellular biology · 2014Article
- Lineage-specific function of Engrailed-2 in the progression of chronic myelogenous leukemia to T-cell blast crisis.Cell cycle (Georgetown, Tex.) · 2014Article
- RAG and HMGB1 create a large bend in the 23RSS in the V(D)J recombination synaptic complexes.Nucleic acids research · 2013Article
- HMGB1: A Promising Therapeutic Target for Prostate Cancer.Prostate cancer · 2013Article
- HMGB1: The Central Cytokine for All Lymphoid Cells.Frontiers in immunology · 2013Article
- HMGB1: a multifunctional alarmin driving autoimmune and inflammatory disease.Nature reviews. Rheumatology · 2012Review
- HMGB1 is a therapeutic target for sterile inflammation and infection.Annual review of immunology · 2011Review
- Structural analysis of HMGD-DNA complexes reveals influence of intercalation on sequence selectivity and DNA bending.Journal of molecular biology · 2010Article
- Chromatin-dependent binding of the S. cerevisiae HMGB protein Nhp6A affects nucleosome dynamics and transcription.Genes & development · 2010Article
- Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis.Nature structural & molecular biology · 2009Article
- Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Efficient assembly of RAG1/2-recombination signal sequence (RSS) DNA complexes that are competent for V(D)J cleavage requires the presence of the nonspecific DNA binding and bending protein HMGB1 or HMGB2. We find that either of the two minimal DNA binding domains of HMGB1 is effective in assembling RAG1/2-RSS complexes on naked DNA and stimulating V(D)J cleavage but that both domains are required for efficient activity when the RSS is incorporated into a nucleosome. The single-domain HMGB protein from Saccharomyces cerevisiae, Nhp6A, efficiently assembles RAG1/2 complexes on naked DNA; however, these complexes are minimally competent for V(D)J cleavage. Nhp6A forms much more stable DNA complexes than HMGB1, and a variety of mutations that destabilize Nhp6A binding to bent microcircular DNA promote increased V(D)J cleavage. One of the two DNA bending wedges on Nhp6A and the analogous phenylalanine wedge at the DNA exit site of HMGB1 domain A were found to be essential for promoting RAG1/2-RSS complex formation. Because the phenylalanine wedge is required for specific recognition of DNA kinks, we propose that HMGB proteins facilitate RAG1/2-RSS interactions by recognizing a distorted DNA structure induced by RAG1/2 binding. The resulting complex must be sufficiently dynamic to enable the series of RAG1/2-mediated chemical reactions on the DNA.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.