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The role of meiosis-specific cohesins in accurate chromosome segregation

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TitleInfo
Title
The role of meiosis-specific cohesins in accurate chromosome segregation
Name (type = personal)
NamePart (type = family)
Gyuricza
NamePart (type = given)
Mercedes R.
NamePart (type = date)
1989-
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Mercedes R. Gyuricza
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RoleTerm (authority = RULIB)
author
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Mckim
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Kim
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Kim Mckim
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Advisory Committee
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chair
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Schindler
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Karen
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Karen Schindler
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Advisory Committee
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internal member
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Steward
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Ruth
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Ruth Steward
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Advisory Committee
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internal member
Name (type = personal)
NamePart (type = family)
Gartenberg
NamePart (type = given)
Marc
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Marc Gartenberg
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Advisory Committee
Role
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outside member
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Rutgers University
Role
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degree grantor
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NamePart
Graduate School - New Brunswick
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school
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Text
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theses
OriginInfo
DateCreated (qualifier = exact)
2017
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2017-05
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2017
Place
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xx
Language
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eng
Abstract (type = abstract)
Haploid gametes are formed by a specialized cell division called meiosis. During meiosis there is one round of DNA replication, but two rounds of DNA segregation which leaves the daughter cells with half the amount of DNA as the parents. This special division is highly regulated to ensure that exactly one copy of each chromosome is included in each gamete. Once replicated the sister chromatids are held together by cohesion, and the homologous pairs are held together by the synaptonemal complex (SC). Without either of these two complexes, the chromosomes do not segregate properly at meiosis I. Mitotic cohesin is comprised of four subunits SMC1/SMC3/SCC1/SCC3, which form a ring. However, in many organisms there are meiosis specific cohesin subunits that have been discovered, such as Rec8 that substitutes for SCC1. This dissertation aims to gain insight into the meiosis specific complexes in Drosophila. There is evidence for two meiosis specific cohesin complexes functioning in Drosophila. One of the complexes is comprised of SMC1/SMC3/SOLO/SUNN. This complex has a minor role in SC assembly, but, is required for sister centromere cohesion. The other complex demonstrated is SMC1/SMC3/C(2)M/SA and is primarily responsible for SC assembly, is not involved in sister centromere cohesion and, is highly dynamic. To confirm this complex forms cohesin rings, we have made point mutations within the regions of C(2)M which are thought to mediate interactions with SMC1 and SMC3. The data collected from these mutations, to date, reveals that N-terminal amino acid residues may not be important. We are working to learn if there are alternate roles for C(2)M outside of interacting with the SMCs or if the interface between the SMCs and C(2)M is different than proposed.
Subject (authority = RUETD)
Topic
Microbiology and Molecular Genetics
Subject (authority = ETD-LCSH)
Topic
Meiosis
RelatedItem (type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
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ETD_8079
PhysicalDescription
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electronic resource
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application/pdf
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text/xml
Extent
1 online resource (ix, 124 p. : ill.)
Note (type = degree)
Ph.D.
Note (type = bibliography)
Includes bibliographical references
Note (type = statement of responsibility)
by Mercedes R. Gyuricza
RelatedItem (type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier (type = local)
rucore19991600001
Location
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NjNbRU
Identifier (type = doi)
doi:10.7282/T39G5QP8
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
Gyuricza
GivenName
Mercedes
MiddleName
R.
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2017-04-17 10:44:16
AssociatedEntity
Name
Mercedes Gyuricza
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.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
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2017-04-21T14:16:20
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2017-04-21T14:16:20
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