Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Conditional RAG-1 mutants block the hairpin formation step of V(D)J recombination.

Molecular and cellular biology - 1 Jan 2001

Kale S B, Landree M A, Roth D B

Abstract excerpt

Hairpin formation serves an important regulatory role in V(D)J recombination because it requires synapsis of an appropriate pair of recombination sites. How hairpin formation is regulated and which regions of the RAG proteins perform this step remain unknown. We analyzed two conditional RAG-1 mutants that affect residues quite close in the primary sequence to an active site amino acid (D600), and we found that...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Substitution
Share to Base Pairing
Share to Gene Rearrangement

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Homeodomain Proteins

Share to Nucleic Acid Conformation

Share to Oligodeoxyribonucleotides

Share to Protein Structure, Tertiary

Share to Recombination, Genetic

Source

Open in PubMed Open full text

Identifiers

PMID: 11134334
DOI: 10.1128/MCB.21.2.459-466.2001
PMCID: PMC86598

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Conditional RAG-1 mutants block the hairpin formation step of V(D)J recombination.PMID 11134334Read ↗

Mutational analysis of all conserved basic amino acids in RAG-1 reveals catalytic, step arrest, and joining-deficient mutants in the V(D)J recombinase.Semantic proximity Read ↗

Understanding how the V(D)J recombinase catalyzes transesterification: distinctions between DNA cleavage and transposition.Semantic proximity Read ↗

Requirements for DNA hairpin formation by RAG1/2.Semantic proximity Read ↗

Evidence of a critical architectural function for the RAG proteins in end processing, protection, and joining in V(D)J recombination.Semantic proximity Read ↗

The DDE motif in RAG-1 is contributed in trans to a single active site that catalyzes the nicking and transesterification steps of V(D)J recombination.Semantic proximity Read ↗

Identification and characterization of a gain-of-function RAG-1 mutant.Semantic proximity Read ↗

Detection of RAG protein-V(D)J recombination signal interactions near the site of DNA cleavage by UV cross-linking.Semantic proximity Read ↗

Impairment of V(D)J recombination in double-strand break repair mutants.Semantic proximity Read ↗

Autoinhibition of DNA cleavage mediated by RAG1 and RAG2 is overcome by an epigenetic signal in V(D)J recombination.Semantic proximity Read ↗

Hairpin coding end opening is mediated by RAG1 and RAG2 proteins.Semantic proximity Read ↗

Crystal structure of the V(D)J recombinase RAG1-RAG2.Semantic proximity Read ↗

Elements between the IgH variable (V) and diversity (D) clusters influence antisense transcription and lineage-specific V(D)J recombination.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.