Early steps of V(D)J rearrangement: Insights from biochemical studies of RAG-RSS complexes

Patrick C. Swanson; Sushi Kumar; Prafulla Raval

doi:10.1007/978-1-4419-0296-2_1

Early steps of V(D)J rearrangement: Insights from biochemical studies of RAG-RSS complexes

Patrick C. Swanson, Sushi Kumar, Prafulla Raval

Department of Medical Microbiology and Immunology

Research output: Chapter in Book/Report/Conference proceeding › Chapter

13 Scopus citations

Abstract

V:(D)J recombinationis initiated by the synapsis and cleavage of a complementary(12123) pair of recombination signalsequences (RSSs) by the RAG1 and RAG2 proteins. Our understanding of these processes has been greadyaided by the development of in vitro biochemicalassays of RAG binding and cleavage activity. Accumulating evidencesuggests that synapticcomplexassembly occursin a step-wise manner and that the RAG proteins catalyze RSS cleavage by mechanisms similar to those used by bacterial transposases. In this chapter we will reviewthe molecularmechanisms of RAG synapticcomplexassembly and 12123-regulated RSS cleavage, focusingon recent advances that shed newlight on theseprocesses.

Original language	English (US)
Title of host publication	V(D)J Recombination
Editors	Pierre Ferrier
Pages	1-15
Number of pages	15
DOIs	https://doi.org/10.1007/978-1-4419-0296-2_1
State	Published - 2009

Publication series

Name	Advances in Experimental Medicine and Biology
Volume	650
ISSN (Print)	0065-2598

All Science Journal Classification (ASJC) codes

Biochemistry, Genetics and Molecular Biology(all)

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10.1007/978-1-4419-0296-2_1

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abstract = "V:(D)J recombinationis initiated by the synapsis and cleavage of a complementary(12123) pair of recombination signalsequences (RSSs) by the RAG1 and RAG2 proteins. Our understanding of these processes has been greadyaided by the development of in vitro biochemicalassays of RAG binding and cleavage activity. Accumulating evidencesuggests that synapticcomplexassembly occursin a step-wise manner and that the RAG proteins catalyze RSS cleavage by mechanisms similar to those used by bacterial transposases. In this chapter we will reviewthe molecularmechanisms of RAG synapticcomplexassembly and 12123-regulated RSS cleavage, focusingon recent advances that shed newlight on theseprocesses.",

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AB - V:(D)J recombinationis initiated by the synapsis and cleavage of a complementary(12123) pair of recombination signalsequences (RSSs) by the RAG1 and RAG2 proteins. Our understanding of these processes has been greadyaided by the development of in vitro biochemicalassays of RAG binding and cleavage activity. Accumulating evidencesuggests that synapticcomplexassembly occursin a step-wise manner and that the RAG proteins catalyze RSS cleavage by mechanisms similar to those used by bacterial transposases. In this chapter we will reviewthe molecularmechanisms of RAG synapticcomplexassembly and 12123-regulated RSS cleavage, focusingon recent advances that shed newlight on theseprocesses.

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Early steps of V(D)J rearrangement: Insights from biochemical studies of RAG-RSS complexes

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