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The role of meiosis-specific cohesins in accurate chromosome segregation
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Gyuricza, Mercedes R.. The role of meiosis-specific cohesins in accurate chromosome segregation. Retrieved from https://doi.org/doi:10.7282/T39G5QP8

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TitleThe role of meiosis-specific cohesins in accurate chromosome segregation
NameGyuricza, Mercedes R. (author); Mckim, Kim (chair); Schindler, Karen (internal member); Steward, Ruth (internal member); Gartenberg, Marc (outside member); Rutgers University; Graduate School - New Brunswick
Date Created2017
Other Date2017-05 (degree)
SubjectMicrobiology and Molecular Genetics, Meiosis
Extent1 online resource (ix, 124 p. : ill.)
DescriptionHaploid 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.
NotePh.D.
NoteIncludes bibliographical references
Noteby Mercedes R. Gyuricza
Genretheses, ETD doctoral
Persistent URLhttps://doi.org/doi:10.7282/T39G5QP8
Languageeng
CollectionGraduate School - New Brunswick Electronic Theses and Dissertations
Organization NameRutgers, The State University of New Jersey
RightsThe author owns the copyright to this work.
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