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Regulation of V(D)J recombination at...

Ross, Ashley E.

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Regulation of V(D)J recombination at the levels of recombinase activity and locus accessibility.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Regulation of V(D)J recombination at the levels of recombinase activity and locus accessibility./
Author:	Ross, Ashley E.
Description:	170 p.
Notes:	Source: Dissertation Abstracts International, Volume: 67-04, Section: B, page: 1837.
Contained By:	Dissertation Abstracts International67-04B.
Subject:	Biology, Molecular. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3213790
ISBN:	9780542644917

Regulation of V(D)J recombination at the levels of recombinase activity and locus accessibility.
Ross, Ashley E.

Regulation of V(D)J recombination at the levels of recombinase activity and locus accessibility. - 170 p.

Source: Dissertation Abstracts International, Volume: 67-04, Section: B, page: 1837.

Thesis (Ph.D.)--The Johns Hopkins University, 2006.

Antigen receptor genes are encoded in separate DNA segments that are brought together during lymphoid development by V(D)J recombination, the only form of site-specific DNA recombination known in vertebrates and the principal means by which immunologic diversity is generated in mammals. V(D)J recombination is highly regulated, both at the level of the recombinase itself (composed of RAG-1 and RAG-2 proteins) and at the level of substrate accessibility. V(D)J is limited to the G0/G1 cell cycle phases by the periodic destruction of RAG-2 at the G1-S transition. Degradation of RAG-2 is mediated by a conserved interval in the recombination-dispensable region. Here we show that RAG-2 degradation in vivo is mediated by ubiquitylation and proteasomal destruction. By generating transgenic animals expressing a mutant form of RAG-2, which is not degraded within the cell cycle, we demonstrate that cell cycle dependent degradation of RAG-2 is not critical for the maintenance of allelic exclusion. Furthermore, we define a nuclear localization signal within RAG-2 that overlaps signals for degradation and bring evidence that RAG-2 intrinsic nuclear uptake plays a role in maintaining efficient levels of recombination in cycling cells.

ISBN: 9780542644917Subjects--Topical Terms:

1017719
Biology, Molecular.

Regulation of V(D)J recombination at the levels of recombinase activity and locus accessibility.
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035 $a (UnM)AAI3213790
035 $a AAI3213790
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100 1 $a Ross, Ashley E. $3 1920615
245 1 0 $a Regulation of V(D)J recombination at the levels of recombinase activity and locus accessibility.
300 $a 170 p.
500 $a Source: Dissertation Abstracts International, Volume: 67-04, Section: B, page: 1837.
500 $a Adviser: Steven Desiderio.
502 $a Thesis (Ph.D.)--The Johns Hopkins University, 2006.
520 $a Antigen receptor genes are encoded in separate DNA segments that are brought together during lymphoid development by V(D)J recombination, the only form of site-specific DNA recombination known in vertebrates and the principal means by which immunologic diversity is generated in mammals. V(D)J recombination is highly regulated, both at the level of the recombinase itself (composed of RAG-1 and RAG-2 proteins) and at the level of substrate accessibility. V(D)J is limited to the G0/G1 cell cycle phases by the periodic destruction of RAG-2 at the G1-S transition. Degradation of RAG-2 is mediated by a conserved interval in the recombination-dispensable region. Here we show that RAG-2 degradation in vivo is mediated by ubiquitylation and proteasomal destruction. By generating transgenic animals expressing a mutant form of RAG-2, which is not degraded within the cell cycle, we demonstrate that cell cycle dependent degradation of RAG-2 is not critical for the maintenance of allelic exclusion. Furthermore, we define a nuclear localization signal within RAG-2 that overlaps signals for degradation and bring evidence that RAG-2 intrinsic nuclear uptake plays a role in maintaining efficient levels of recombination in cycling cells.
520 $a In another study, we characterize the properties of the signal end complex, an intermediate product in the recombination reaction formed between the RAGS and cleaved signal ends that has been shown to mediate transposition in vitro. We isolate signal end complexes formed intracellularly with either full-length RAG proteins or their core truncation mutants and demonstrate that complexes containing full-length RAG proteins transpose signal end flanked DNA with similar efficiency and target site specificity as those containing the core RAG proteins.
520 $a Finally, we study the signaling pathways down stream of the pre-B cell receptor. Using a activated form of the tyrosine kinase Blk, we demonstrate that activation of Blk can effect a suite of responses normally associated with the pre-BCR including the stimulation of proliferation and development, and the control of locus accessibility by suppression of heavy chain and activation of light chain rearrangement.
590 $a School code: 0098.
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Health Sciences, Immunology. $3 1017716
690 $a 0307
690 $a 0487
690 $a 0982
710 2 0 $a The Johns Hopkins University. $3 1017431
773 0 $t Dissertation Abstracts International $g 67-04B.
790 1 0 $a Desiderio, Steven, $e advisor
790 $a 0098
791 $a Ph.D.
792 $a 2006
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3213790