Mutational analysis of RAG1 and RAG2 identifies three catalytic amino acids in RAG1 critical for both cleavage steps of V(D)J recombination. - Wikidata - wikimedia - TriplyDB

Mutational analysis of RAG1 and RAG2 identifies three catalytic amino acids in RAG1 critical for both cleavage steps of V(D)J recombination.

Mutational analysis of RAG1 and RAG2 identifies three catalytic amino acids in RAG1 critical for both cleavage steps of V(D)J recombination.

http://www.wikidata.org/entity/Q35210006

about

RAG1 core and V(D)J recombination signal sequences were derived from Transib transposons Amino acid residues in RAG1 responsible for the interaction with RAG2 during the V(D)J recombination process An ancient evolutionary origin of the Rag1/2 gene locus The recombination activation gene 1 (Rag1) is expressed in a subset of zebrafish olfactory neurons but is not essential for axon targeting or amino acid detection.Long-Range Regulation of V(D)J Recombination Retroviral Integrase: Then and Now Putting the pieces together: identification and characterization of structural domains in the V(D)J recombination protein RAG1 Recombination-activating gene proteins: more regulation, please The taming of a transposon: V(D)J recombination and the immune system Human RAG mutations: biochemistry and clinical implications RAG-1 and ATM coordinate monoallelic recombination and nuclear positioning of immunoglobulin loci Autoubiquitylation of the V(D)J recombinase protein RAG1 Mutations of acidic residues in RAG1 define the active site of the V(D)J recombinase Compound heterozygous mutation of Rag1 leading to Omenn syndrome A WW-like module in the RAG1 N-terminal domain contributes to previously unidentified protein-protein interactions Genomic DNA transposition induced by human PGBD5 Adapting to a changing world: RAG genomics and evolution Functional characterization of an active Rag-like transposase Crystal structure of the V(D)J recombinase RAG1-RAG2 Elucidating 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 binding Self-association and conformational properties of RAG1: implications for formation of the V(D)J recombinase.Thermal dependency of RAG1 self-association properties.Mutational analysis of highly conserved aspartate residues essential to the catalytic core of the piggyBac transposase RAG2's acidic hinge restricts repair-pathway choice and promotes genomic stability.The origins of the Rag genes--from transposition to V(D)J recombination.A family of developmentally excised DNA elements in Tetrahymena is under selective pressure to maintain an open reading frame encoding an integrase-like protein Differential requirements for cis and trans V(D)J cleavage: effects of substrate length Non-consensus heptamer sequences destabilize the RAG post-cleavage complex, making ends available to alternative DNA repair pathways.The in vivo pattern of binding of RAG1 and RAG2 to antigen receptor loci.Effect of HIV integrase inhibitors on the RAG1/2 recombinase.Mutations in conserved regions of the predicted RAG2 kelch repeats block initiation of V(D)J recombination and result in primary immunodeficiencies 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 Conditional 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 complexes RAG transposase can capture and commit to target DNA before or after donor cleavage Ordered assembly of the V(D)J synaptic complex ensures accurate recombination The 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 recombinase

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Mutational analysis of RAG1 and RAG2 identifies three catalytic amino acids in RAG1 critical for both cleavage steps of V(D)J recombination.

http://www.wikidata.org/entity/Q35210006

description

1999 nî lūn-bûn

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1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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Mutational analysis of RAG1 an ...... steps of V(D)J recombination.

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Mutational analysis of RAG1 an ...... steps of V(D)J recombination.

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Mutational analysis of RAG1 an ...... steps of V(D)J recombination.

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D B Roth

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J A Wibbenmeyer

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M A Landree

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P2860

High-resolution structure of the catalytic domain of avian sarcoma virus integrase

Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration

The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations

Three new structures of the core domain of HIV-1 integrase: an active site that binds magnesium

Crystal structures of the catalytic domain of HIV-1 integrase free and complexed with its metal cofactor: high level of similarity of the active site with other viral integrases

Rapid and efficient site-specific mutagenesis without phenotypic selection

The RAG1 and RAG2 proteins establish the 12/23 rule in V(D)J recombination

Expression and V(D)J recombination activity of mutated RAG-1 proteins

Mutations of acidic residues in RAG1 define the active site of the V(D)J recombinase

Metal ion catalysis in the Tetrahymena ribozyme reaction

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10.1101/GAD.13.23.3059

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23

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12700448

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10601032

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317185

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