Identification of basic residues in RAG2 critical for DNA binding by the RAG1-RAG2 complex (Q38295277)

1 September 2017

title

Identification of basic residues in RAG2 critical for DNA binding by the RAG1-RAG2 complex (English)

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1 September 2017

Fugmann SD

1

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1 September 2017

Schatz DG

series ordinal

2

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1 September 2017

publication date

1 October 2001

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1 September 2017

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1 September 2017

volume

8

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1 September 2017

issue

4

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1 September 2017

page(s)

899-910

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The kelch repeat superfamily of proteins: propellers of cell function

1 September 2017

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7 January 2021

RAG1 and RAG2 form a stable postcleavage synaptic complex with DNA containing signal ends in V(D)J recombination

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7 January 2021

Transposition mediated by RAG1 and RAG2 and its implications for the evolution of the immune system

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7 January 2021

The RAG1 homeodomain recruits HMG1 and HMG2 to facilitate recombination signal sequence binding and to enhance the intrinsic DNA-bending activity of RAG1-RAG2

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Definition of minimal domains of interaction within the recombination-activating genes 1 and 2 recombinase complex

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7 January 2021

Distinct roles of RAG1 and RAG2 in binding the V(D)J recombination signal sequences

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7 January 2021

The V(D)J recombination activating protein RAG2 consists of a six-bladed propeller and a PHD fingerlike domain, as revealed by sequence analysis

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Three-dimensional clustering of human RAG2 gene mutations in severe combined immune deficiency.

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Analysis of regions of RAG-2 important for V(D)J recombination

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Three-dimensional structure of the Tn5 synaptic complex transposition intermediate

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7 January 2021

RAG1 mediates signal sequence recognition and recruitment of RAG2 in V(D)J recombination

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

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Hin recombinase bound to DNA: the origin of specificity in major and minor groove interactions

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7 January 2021

The RAG proteins and V(D)J recombination: complexes, ends, and transposition

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7 January 2021

Identification of two catalytic residues in RAG1 that define a single active site within the RAG1/RAG2 protein complex.

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7 January 2021

Mutations in conserved regions of the predicted RAG2 kelch repeats block initiation of V(D)J recombination and result in primary immunodeficiencies

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How to make ends meet in V(D)J recombination

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7 January 2021

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Extrachromosomal DNA substrates in pre-B cells undergo inversion or deletion at immunoglobulin V-(D)-J joining signals

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7 January 2021

A stable RAG1-RAG2-DNA complex that is active in V(D)J cleavage

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7 January 2021

Assembly of a 12/23 paired signal complex: a critical control point in V(D)J recombination

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7 January 2021

DNA transposition by the RAG1 and RAG2 proteins: a possible source of oncogenic translocations

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7 January 2021

Functional analysis of coordinated cleavage in V(D)J recombination

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7 January 2021

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

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7 January 2021

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

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7 January 2021

rag-1 and rag-2 are components of a high-molecular-weight complex, and association of rag-2 with this complex is rag-1 dependent

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7 January 2021

The mechanism of V(D)J joining: lessons from molecular, immunological, and comparative analyses

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7 January 2021

Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases

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7 January 2021

Cleavage at a V(D)J recombination signal requires only RAG1 and RAG2 proteins and occurs in two steps

1 reference

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7 January 2021

RAG1 and RAG2 cooperate in specific binding to the recombination signal sequence in vitro

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7 January 2021

A highly ordered structure in V(D)J recombination cleavage complexes is facilitated by HMG1.

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7 January 2021

RAG-1 and RAG-2, adjacent genes that synergistically activate V(D)J recombination

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7 January 2021

Separation-of-function mutants reveal critical roles for RAG2 in both the cleavage and joining steps of V(D)J recombination

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7 January 2021

A dimer of the lymphoid protein RAG1 recognizes the recombination signal sequence and the complex stably incorporates the high mobility group protein HMG2.

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7 January 2021

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

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7 January 2021

Definition of a core region of RAG-2 that is functional in V(D)J recombination

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7 January 2021

The V(D)J recombination activating gene, RAG-1.

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7 January 2021

The homeodomain region of Rag-1 reveals the parallel mechanisms of bacterial and V(D)J recombination

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7 January 2021

A general two-metal-ion mechanism for catalytic RNA

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7 January 2021

V(D)J recombination signal recognition: distinct, overlapping DNA-protein contacts in complexes containing RAG1 with and without RAG2.

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7 January 2021

RAG-2 promotes heptamer occupancy by RAG-1 in the assembly of a V(D)J initiation complex

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7 January 2021

Somatic generation of antibody diversity

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7 January 2021

Initiation of V(D)J recombination in a cell-free system.

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https://api.crossref.org/works/10.1016%2FS1097-2765%2801%2900352-5

7 January 2021

10.1016/S1097-2765(01)00352-5

Identifiers

DOI

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1 September 2017

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