RAG and HMGB1 proteins: purification and biochemical analysis of recombination signal complexes. (Q53616216)

16 May 2018

title

RAG and HMGB1 proteins: purification and biochemical analysis of recombination signal complexes. (English)

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16 May 2018

author name string

Serge Bergeron

series ordinal

1

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16 May 2018

Dirk K Anderson

series ordinal

2

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16 May 2018

Patrick C Swanson

series ordinal

3

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16 May 2018

language of work or name

English

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publication date

1 January 2006

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16 May 2018

published in

Methods in Enzymology

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16 May 2018

volume

408

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16 May 2018

page(s)

511-528

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16 May 2018

Deletion of the RAG2 C terminus leads to impaired lymphoid development in mice

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Both high mobility group (HMG)-boxes and the acidic tail of HMGB1 regulate recombination-activating gene (RAG)-mediated recombination signal synapsis and cleavage in vitro

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A short peptide at the C terminus is responsible for the nuclear localization of RAG2.

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

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The C-terminal portion of RAG2 protects against transposition in vitro

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

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V(D)J recombination: RAG proteins, repair factors, and regulation

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

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Cell cycle-dependent accumulation in vivo of transposition-competent complexes between recombination signal ends and full-length RAG proteins

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Lack of N regions in antigen receptor variable region genes of TdT-deficient lymphocytes

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A conserved degradation signal regulates RAG-2 accumulation during cell division and links V(D)J recombination to the cell cycle

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RAG2 is down-regulated by cytoplasmic sequestration and ubiquitin-dependent degradation

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Assembly of the RAG1/RAG2 synaptic complex

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

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Overlapping signals for protein degradation and nuclear localization define a role for intrinsic RAG-2 nuclear uptake in dividing cells

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

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V(D)J recombination: modulation of RAG1 and RAG2 cleavage activity on 12/23 substrates by whole cell extract and DNA-bending proteins

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Increased accumulation of hybrid V(D)J joins in cells expressing truncated versus full-length RAGs.

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

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7 January 2021

Roles of the "dispensable" portions of RAG-1 and RAG-2 in V(D)J recombination

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7 January 2021

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

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7 January 2021

Fine structure and activity of discrete RAG-HMG complexes on V(D)J recombination signals

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7 January 2021

A RAG-1/RAG-2 tetramer supports 12/23-regulated synapsis, cleavage, and transposition of V(D)J recombination signals

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Full-length RAG-2, and Not Full-length RAG-1, Specifically Suppresses RAG-mediated Transposition but Not Hybrid Joint Formation or Disintegration

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Increased frequency of aberrant V(D)J recombination products in core RAG-expressing mice

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HMG1 and 2, and related 'architectural' DNA-binding proteins

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Regulation of RAG1/RAG2-mediated transposition by GTP and the C-terminal region of RAG2

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Stimulation of V(D)J cleavage by high mobility group proteins

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7 January 2021

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The RAG1 N-terminal domain is an E3 ubiquitin ligase

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Identifiers

DOI

1 reference

16 May 2018

PubMed ID

16793390

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16 May 2018