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The nucleosome as a potential barrie...

Golding, Amit.

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The nucleosome as a potential barrier to the V(D)J recombinase.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	The nucleosome as a potential barrier to the V(D)J recombinase./
Author:	Golding, Amit.
Description:	135 p.
Notes:	Advisers: Mark Schlissel; Stephen Desiderio.
Contained By:	Dissertation Abstracts International63-03B.
Subject:	Biology, Genetics. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3046459
ISBN:	0493606491

The nucleosome as a potential barrier to the V(D)J recombinase.
Golding, Amit.

The nucleosome as a potential barrier to the V(D)J recombinase. - 135 p.

Advisers: Mark Schlissel; Stephen Desiderio.

Thesis (Ph.D.)--The Johns Hopkins University, 2002.

Lineage specificity and temporal ordering of immunoglobulin (Ig) and T cell receptor (TCR) gene rearrangement are reflected in the accessibility of recombination signal sequences (RSSs) within chromatin to in vitro cleavage by the V(D)J recombinase. In the present work, I investigated the basis of this regulation by testing the ability of purified RAG1 and RAG2 proteins to initiate cleavage on positioned nucleosomes containing RSS substrates. I found that nicking and double-strand DNA cleavage of RSSs positioned on the face of an unmodified nucleosome are entirely inhibited. This inhibition was independent of translational position or rotational phase and could not be overcome either by addition of the DNA-bending protein HMG-1 or by the use of hyperacetylated histones. I suggest that the nucleosome could act as the stable unit of chromatin that limits recombinase accessibility to potential RSS targets, and that actively rearranging gene segments might be packaged in a modified or disrupted nucleosome structure. Using techniques based on MNase and restriction enzyme digestion of intact nuclei, I examined the in vivo chromatin structure of the immunoglobulin kappa locus J genes in non-lymphoid cells as compared to lymphoid cells poised at different stages of development. I present preliminary data from general MNase sensitivity, indirect end-labeling, high resolution mapping of MNase breaks by LMPCR, and restriction enzyme accessibility.

ISBN: 0493606491Subjects--Topical Terms:

1017730
Biology, Genetics.

The nucleosome as a potential barrier to the V(D)J recombinase.
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035 $a (UnM)AAI3046459
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100 1 $a Golding, Amit. $3 1251256
245 1 0 $a The nucleosome as a potential barrier to the V(D)J recombinase.
300 $a 135 p.
500 $a Advisers: Mark Schlissel; Stephen Desiderio.
500 $a Source: Dissertation Abstracts International, Volume: 63-03, Section: B, page: 1169.
502 $a Thesis (Ph.D.)--The Johns Hopkins University, 2002.
520 $a Lineage specificity and temporal ordering of immunoglobulin (Ig) and T cell receptor (TCR) gene rearrangement are reflected in the accessibility of recombination signal sequences (RSSs) within chromatin to in vitro cleavage by the V(D)J recombinase. In the present work, I investigated the basis of this regulation by testing the ability of purified RAG1 and RAG2 proteins to initiate cleavage on positioned nucleosomes containing RSS substrates. I found that nicking and double-strand DNA cleavage of RSSs positioned on the face of an unmodified nucleosome are entirely inhibited. This inhibition was independent of translational position or rotational phase and could not be overcome either by addition of the DNA-bending protein HMG-1 or by the use of hyperacetylated histones. I suggest that the nucleosome could act as the stable unit of chromatin that limits recombinase accessibility to potential RSS targets, and that actively rearranging gene segments might be packaged in a modified or disrupted nucleosome structure. Using techniques based on MNase and restriction enzyme digestion of intact nuclei, I examined the in vivo chromatin structure of the immunoglobulin kappa locus J genes in non-lymphoid cells as compared to lymphoid cells poised at different stages of development. I present preliminary data from general MNase sensitivity, indirect end-labeling, high resolution mapping of MNase breaks by LMPCR, and restriction enzyme accessibility.
590 $a School code: 0098.
650 4 $a Biology, Genetics. $3 1017730
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Health Sciences, Immunology. $3 1017716
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690 $a 0369
690 $a 0982
710 2 0 $a The Johns Hopkins University. $3 1017431
773 0 $t Dissertation Abstracts International $g 63-03B.
790 $a 0098
790 1 0 $a Desiderio, Stephen, $e advisor
790 1 0 $a Schlissel, Mark, $e advisor
791 $a Ph.D.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3046459