Structural and Functional Studies of the human cohesin subunits Rad21 and SA2

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dc.contributor.advisorTao, Yizhi Janeen_US
dc.creatorJiang, Yunyunen_US
dc.date.accessioned2013-03-08T00:34:46Zen_US
dc.date.available2013-03-08T00:34:46Zen_US
dc.date.issued2012en_US
dc.description.abstractThe cohesin complex is responsible for the fidelity of chromosomal segregation during mitosis. It consists of four core subunits namely Rad21/Mcd1/Sccl, Smc1, Smc3 and one of the yeast Scc3 orthologs SA1 or SA2. Sister chromatid cohesion is formed by the cohesin complex during DNA replication and maintained until the onset of anaphase. Among the many proposed models of how cohesin holds sister chromatids together, the 'core' cohesin subunits Smc1, Smc3 and Rad21/Mcd1/Scc1 are almost universally displayed as forming a contiguous ring. However, other than its supportive role in the cohesin ring, little is known about the fourth core protein SA1/SA2 - despite its physical association to the cohesin ring. To gain deeper insight into how physically and physiologically SA2 interacts with the cohesin complex, we performed structural characterization of SA2 and Rad21 and mapped the interaction region of the two proteins in vitro and ex vivo . We found SA2 interacts with Rad21 at multiple domains while Rad21 only interacts with SA2 through a 10 amino acid α-helical motif from 383-392aa. Deletion of these 10 amino acids or mutation of three conserved amino acids (L385, F389, and T390) in this α-helical motif prevents Rad21 from physically interacting with SA2/SA1 and causes premature sister chromatid separation in mitotic cells that often leads to aneuploidy. Our studies provide a model for how SA2 structurally strengthens the cohesin ring through its interaction with Rad21. Results from our structural characterization of these two proteins also provided directions for further investigation of the structural basis of protein-protein interaction in the cohesin complex.en_US
dc.format.extent150 p.en_US
dc.format.mimetypeapplication/pdfen_US
dc.identifier.callnoTHESIS BIOCHEM. 2012 JIANGen_US
dc.identifier.citationJiang, Yunyun. "Structural and Functional Studies of the human cohesin subunits Rad21 and SA2." (2012) Diss., Rice University. <a href="https://hdl.handle.net/1911/70280">https://hdl.handle.net/1911/70280</a>.en_US
dc.identifier.digitalJiangYen_US
dc.identifier.urihttps://hdl.handle.net/1911/70280en_US
dc.language.isoengen_US
dc.rightsCopyright is held by the author, unless otherwise indicated. Permission to reuse, publish, or reproduce the work beyond the bounds of fair use or other exemptions to copyright law must be obtained from the copyright holder.en_US
dc.subjectHealth sciencesen_US
dc.subjectEnvironmental scienceen_US
dc.subjectPure sciencesen_US
dc.subjectBiological sciencesen_US
dc.subjectCohesinen_US
dc.subjectRad21en_US
dc.subjectSA2en_US
dc.subjectInteractionsen_US
dc.subjectAneuploidyen_US
dc.subjectMitosisen_US
dc.subjectCellular biologyen_US
dc.subjectBiochemistryen_US
dc.subjectOncologyen_US
dc.titleStructural and Functional Studies of the human cohesin subunits Rad21 and SA2en_US
dc.typeThesisen_US
dc.type.materialTexten_US
thesis.degree.departmentBiochemistry and Cell Biologyen_US
thesis.degree.disciplineNatural Sciencesen_US
thesis.degree.grantorRice Universityen_US
thesis.degree.levelDoctoralen_US
thesis.degree.nameDoctor of Philosophyen_US
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