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Genome-wide intergenic repression by polycomb group proteins

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TitleInfo
Title
Genome-wide intergenic repression by polycomb group proteins
Name (type = personal)
NamePart (type = family)
Lee
NamePart (type = given)
Hungoo
NamePart (type = date)
1980-
DisplayForm
Hungoo Lee
Role
RoleTerm (authority = RULIB)
author
Name (type = personal)
NamePart (type = family)
Pirrotta
NamePart (type = given)
Vincenzo
DisplayForm
Vincenzo Pirrotta
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
chair
Name (type = personal)
NamePart (type = family)
Edery
NamePart (type = given)
Isaac
DisplayForm
Isaac Edery
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Hampsey
NamePart (type = given)
Michael
DisplayForm
Michael Hampsey
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Gartenberg
NamePart (type = given)
Marc
DisplayForm
Marc Gartenberg
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
outside member
Name (type = corporate)
NamePart
Rutgers University
Role
RoleTerm (authority = RULIB)
degree grantor
Name (type = corporate)
NamePart
Graduate School - New Brunswick
Role
RoleTerm (authority = RULIB)
school
TypeOfResource
Text
Genre (authority = marcgt)
theses
OriginInfo
DateCreated (qualifier = exact)
2014
DateOther (qualifier = exact); (type = degree)
2014-01
Place
PlaceTerm (type = code)
xx
Language
LanguageTerm (authority = ISO639-2b); (type = code)
eng
Abstract (type = abstract)
Polycomb group (PcG) proteins have been studied as epigenetic regulators of diverse developmental regulatory genes in various organisms. PcG proteins form two major complexes: the Polycomb repressive complex 2 (PRC2) which includes Enhancer of zeste (E(Z)) that methylates the lysine 27 residue of histone H3 (H3K27) and the Polycomb repressive complex 1 (PRC1) which preferentially binds to tri-methylated H3K27 (H3K27me3). Recent genome-wide analysis revealed that the PcG proteins stably bind to hundreds of genomic loci with strong H3K27me3 enrichment. Unlike the focused enrichment of H3K27me3, di-methylation of H3K27 (H3 K27me2) is found on more than half of all nucleosomal H3, raising the interesting possibility that H3K27me2 might have a potential repressive role across the genome. To address the possibility, we generated an E(z) temperature sensitive mutant cell line and examined the effects of E(Z) inactivation. Upon E(Z) inactivation, we observed a strong transcriptional increase from the H3K27me2-enriched intergenic regions along with significant increases of H3K27ac and H3K4me1. The intergenic de-repression was dependent on two dUTX-containing H3K27 de-methylase complexes that are associated with the increased active marks. Genome-wide analysis revealed that these effects are prevailing all over the genome, suggesting an antagonistic relationship between PRC2 and the dUTX complexes for regulating chromatin states genome-wide. In addition, PRC1 involvement in the intergenic repression was indicated by increased intergenic transcription by knock-downs or a mutation of PRC1 components. Moreover, a significant level of H2Aub1, a repressive mark produced by PRC1, was found in silent intergenic regions. These results extend the roles of PcG proteins by showing that PcG complexes not only function as master regulators of several hundred developmental regulators but also set a high inhibitory threshold to suppress the pervasive intergenic transcription all over the genome.
Subject (authority = RUETD)
Topic
Biochemistry
RelatedItem (type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
Identifier
ETD_5226
PhysicalDescription
Form (authority = gmd)
electronic resource
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
x, 132 p. : ill.
Note (type = degree)
Ph.D.
Note (type = bibliography)
Includes bibliographical references
Note (type = statement of responsibility)
by Hungoo Lee
Subject (authority = ETD-LCSH)
Topic
Protein engineering
Subject (authority = ETD-LCSH)
Topic
Genomes
Subject (authority = ETD-LCSH)
Topic
Genomics
RelatedItem (type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier (type = local)
rucore19991600001
Location
PhysicalLocation (authority = marcorg); (displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier (type = doi)
doi:10.7282/T3251G86
Genre (authority = ExL-Esploro)
ETD doctoral
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Rights

RightsDeclaration (ID = rulibRdec0006)
The author owns the copyright to this work.
RightsHolder (type = personal)
Name
FamilyName
Lee
GivenName
Hungoo
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2013-12-18 16:30:24
AssociatedEntity
Name
Hungoo Lee
Role
Copyright holder
Affiliation
Rutgers University. Graduate School - New Brunswick
AssociatedObject
Type
License
Name
Author Agreement License
Detail
I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
RightsEvent
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2014-01-31
DateTime (encoding = w3cdtf); (qualifier = exact); (point = end)
2016-01-31
Type
Embargo
Detail
Access to this PDF has been restricted at the author's request. It will be publicly available after January 31st, 2016.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
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Technical

RULTechMD (ID = TECHNICAL1)
ContentModel
ETD
OperatingSystem (VERSION = 5.1)
windows xp
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