RAG-2 promotes heptamer occupancy by RAG-1 in the assembly of a V(D)J initiation complex.
about
Amino acid residues in RAG1 responsible for the interaction with RAG2 during the V(D)J recombination processA functional analysis of the spacer of V(D)J recombination signal sequencesStructure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsisPutting the pieces together: identification and characterization of structural domains in the V(D)J recombination protein RAG1The taming of a transposon: V(D)J recombination and the immune systemMapping and Quantitation of the Interaction between the Recombination Activating Gene Proteins RAG1 and RAG2.Crystal structure of the V(D)J recombinase RAG1-RAG2Elucidating the domain architecture and functions of non-core RAG1: the capacity of a non-core zinc-binding domain to function in nuclear import and nucleic acid bindingSelf-association and conformational properties of RAG1: implications for formation of the V(D)J recombinase.Non-consensus heptamer sequences destabilize the RAG post-cleavage complex, making ends available to alternative DNA repair pathways.Mechanistic basis for coding end sequence effects in the initiation of V(D)J recombinationMutations in conserved regions of the predicted RAG2 kelch repeats block initiation of V(D)J recombination and result in primary immunodeficienciesThe 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 recombinationConditional RAG-1 mutants block the hairpin formation step of V(D)J recombination.A C-terminal region of RAG1 contacts the coding DNA during V(D)J recombination.Rag-1 mutations associated with B-cell-negative scid dissociate the nicking and transesterification steps of V(D)J recombination.Functional organization of single and paired V(D)J cleavage complexesOrdered assembly of the V(D)J synaptic complex ensures accurate recombinationThe RAG proteins in V(D)J recombination: more than just a nuclease.Mutational analysis of all conserved basic amino acids in RAG-1 reveals catalytic, step arrest, and joining-deficient mutants in the V(D)J recombinaseAssembly of the RAG1/RAG2 synaptic complexA RAG-1/RAG-2 tetramer supports 12/23-regulated synapsis, cleavage, and transposition of V(D)J recombination signals.The architecture of the 12RSS in V(D)J recombination signal and synaptic complexes.Overlapping signals for protein degradation and nuclear localization define a role for intrinsic RAG-2 nuclear uptake in dividing cells.Mutational analysis of RAG1 and RAG2 identifies three catalytic amino acids in RAG1 critical for both cleavage steps of V(D)J recombination.DNA cleavage activity of the V(D)J recombination protein RAG1 is autoregulated.The molecular basis and biological significance of VH replacement.In vitro and in vivo studies on the generation of the primary T-cell receptor repertoire.Regulation of T-cell receptor beta-chain gene assembly by recombination signals: the beyond 12/23 restriction.The bounty of RAGs: recombination signal complexes and reaction outcomes.Real-time monitoring of RAG-catalyzed DNA cleavage unveils dynamic changes in coding end association with the coding end complex.Understanding how the V(D)J recombinase catalyzes transesterification: distinctions between DNA cleavage and transposition.The PHD domain of the sea urchin RAG2 homolog, SpRAG2L, recognizes dimethylated lysine 4 in histone H3 tailsA plant homeodomain in RAG-2 that binds Hypermethylated lysine 4 of histone H3 is necessary for efficient antigen-receptor-gene rearrangement.Keep your fingers off my DNA: protein-protein interactions mediated by C2H2 zinc finger domains.Quantitative analyses of RAG-RSS interactions and conformations revealed by atomic force microscopy.A non-sequence-specific DNA binding mode of RAG1 is inhibited by RAG2Karyopherin alpha 1 is a putative substrate of the RAG1 ubiquitin ligase.Ordered DNA release and target capture in RAG transpositionInitial stages of V(D)J recombination: the organization of RAG1/2 and RSS DNA in the postcleavage complex.
P2860
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P2860
RAG-2 promotes heptamer occupancy by RAG-1 in the assembly of a V(D)J initiation complex.
description
1999 nî lūn-bûn
@nan
1999 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
RAG-2 promotes heptamer occupancy by RAG-1 in the assembly of a V(D)J initiation complex.
@ast
RAG-2 promotes heptamer occupancy by RAG-1 in the assembly of a V(D)J initiation complex.
@en
type
label
RAG-2 promotes heptamer occupancy by RAG-1 in the assembly of a V(D)J initiation complex.
@ast
RAG-2 promotes heptamer occupancy by RAG-1 in the assembly of a V(D)J initiation complex.
@en
prefLabel
RAG-2 promotes heptamer occupancy by RAG-1 in the assembly of a V(D)J initiation complex.
@ast
RAG-2 promotes heptamer occupancy by RAG-1 in the assembly of a V(D)J initiation complex.
@en
P2860
P356
P1476
RAG-2 promotes heptamer occupancy by RAG-1 in the assembly of a V(D)J initiation complex.
@en
P2093
P C Swanson
S Desiderio
P2860
P304
P356
10.1128/MCB.19.5.3674
P407
P577
1999-05-01T00:00:00Z