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You searched for +publisher:"Vanderbilt University" +contributor:("Ellen H. Fanning"). Showing records 1 – 3 of 3 total matches.

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Vanderbilt University

1. Bohnert, Kenneth Adam. Divide and Prosper: Molecular Mechanisms and Consequences of Cytokinetic Ring Regulation.

Degree: PhD, Cell and Developmental Biology, 2013, Vanderbilt University

In many organisms, a cytokinetic ring directs daughter cell separation following mitosis. While conserved molecular participants in this process have been defined, the signaling events controlling cytokinetic ring function remain obscure. Using a genetically-tractable fission yeast, Schizosaccharomyces pombe, I have investigated mechanisms involved in such signaling, with a particular interest in kinase and phosphatase networks. Through identification of a new subunit of the S. pombe chromosomal passenger complex, I have found that Aurora B kinase influences cytokinesis by mediating Cdc14-family phosphatase accumulation at the cytokinetic ring. In addition, I have discovered that Sid2, a kinase of the S. pombe septation initiation network, phosphorylates cytokinetic formin Cdc12 to reverse formin multimerization and allow cytokinetic ring maintenance. My studies also indicate that cytokinesis impacts cell cycle-dependent polarized growth, and that phosphosignaling at the cytokinetic ring ensures robust growth following cell division. These studies advance our understanding of molecular cues regulating cytokinesis, and broaden knowledge concerning the consequences of this control. Advisors/Committee Members: Kathleen L. Gould (committee member), Stephen R. Hann (committee member), Matthew J. Tyska (committee member), Ellen H. Fanning (committee member), Susan R. Wente (Committee Chair).

Subjects/Keywords: cytokinesis; cell growth; phosphorylation; formin; kinase; morphogenesis

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APA (6th Edition):

Bohnert, K. A. (2013). Divide and Prosper: Molecular Mechanisms and Consequences of Cytokinetic Ring Regulation. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://hdl.handle.net/1803/13123

Chicago Manual of Style (16th Edition):

Bohnert, Kenneth Adam. “Divide and Prosper: Molecular Mechanisms and Consequences of Cytokinetic Ring Regulation.” 2013. Doctoral Dissertation, Vanderbilt University. Accessed January 22, 2021. http://hdl.handle.net/1803/13123.

MLA Handbook (7th Edition):

Bohnert, Kenneth Adam. “Divide and Prosper: Molecular Mechanisms and Consequences of Cytokinetic Ring Regulation.” 2013. Web. 22 Jan 2021.

Vancouver:

Bohnert KA. Divide and Prosper: Molecular Mechanisms and Consequences of Cytokinetic Ring Regulation. [Internet] [Doctoral dissertation]. Vanderbilt University; 2013. [cited 2021 Jan 22]. Available from: http://hdl.handle.net/1803/13123.

Council of Science Editors:

Bohnert KA. Divide and Prosper: Molecular Mechanisms and Consequences of Cytokinetic Ring Regulation. [Doctoral Dissertation]. Vanderbilt University; 2013. Available from: http://hdl.handle.net/1803/13123


Vanderbilt University

2. Song, Zhuo. Stochastic modeling of mitochondrial polymerase gamma replication and novel algorithms to enrich rare disease alleles and detect tumor somatic mutations in deep sequencing data.

Degree: PhD, Human Genetics, 2012, Vanderbilt University

The activity of polymerase ã (pol ã) is complicated. To understand how its kinetics values affect the final function of the pol ã, I created a stochastic model of pol ã replication on the single nucleotide incorporation level. Using this model, I analyzed replication pauses of both wild-type and pathogenic mutated pol ã and discovered that the pausing time is proportional to the number of disassociations occurring in each forward step of the pol ã, and studied mitochondrial toxicity caused by nucleoside analogs in antiretroviral treatment. To enrich the yield of rare disease alleles, a probability-based approach, SampleSeq, has been developed to select samples for a targeted resequencing experiment that outperforms over sampling based on genotypes at associated SNPs from GWAS data. To detect somatic mutations, novel algorithms have been developed to detect base substitution and loss of heterozygosity, using next-generation sequencing data for normal-tumor sample pairs. Advisors/Committee Members: Todd I. Edwards (committee member), Ellen H. Fanning (committee member), William S. Bush (committee member), C. William Wester (committee member), Chun Li (Committee Chair), David C. Samuels (Committee Chair).

Subjects/Keywords: tumor somatic mutations; targeted sequencing; NRTI; polymerase gamma; mtDNA replication

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APA (6th Edition):

Song, Z. (2012). Stochastic modeling of mitochondrial polymerase gamma replication and novel algorithms to enrich rare disease alleles and detect tumor somatic mutations in deep sequencing data. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://hdl.handle.net/1803/10702

Chicago Manual of Style (16th Edition):

Song, Zhuo. “Stochastic modeling of mitochondrial polymerase gamma replication and novel algorithms to enrich rare disease alleles and detect tumor somatic mutations in deep sequencing data.” 2012. Doctoral Dissertation, Vanderbilt University. Accessed January 22, 2021. http://hdl.handle.net/1803/10702.

MLA Handbook (7th Edition):

Song, Zhuo. “Stochastic modeling of mitochondrial polymerase gamma replication and novel algorithms to enrich rare disease alleles and detect tumor somatic mutations in deep sequencing data.” 2012. Web. 22 Jan 2021.

Vancouver:

Song Z. Stochastic modeling of mitochondrial polymerase gamma replication and novel algorithms to enrich rare disease alleles and detect tumor somatic mutations in deep sequencing data. [Internet] [Doctoral dissertation]. Vanderbilt University; 2012. [cited 2021 Jan 22]. Available from: http://hdl.handle.net/1803/10702.

Council of Science Editors:

Song Z. Stochastic modeling of mitochondrial polymerase gamma replication and novel algorithms to enrich rare disease alleles and detect tumor somatic mutations in deep sequencing data. [Doctoral Dissertation]. Vanderbilt University; 2012. Available from: http://hdl.handle.net/1803/10702


Vanderbilt University

3. Robertson, Patrick David. Structural biology of the C-terminal domain of eukaryotic replication factor Mcm10.

Degree: PhD, Biological Sciences, 2010, Vanderbilt University

Eukaryotic DNA replication is tightly regulated during the initiation phase to ensure that the genome is copied only once and at the proper time during each cell cycle. During replication initiation, over twenty different proteins are recruited to each origin of replication to denature the DNA duplex and assemble a functional replication fork. Of these, Mcm10 is a DNA binding protein that is recruited to origins in early S-phase and is required for the activation of Mcm2-7, the replicative DNA helicase. Importantly, Mcm10 is necessary for subsequent loading of downstream replication proteins, including DNA polymerase α-primase (pol α), onto chromatin. Mcm10 interacts with single- and double-stranded DNA, pol α, as well as other proteins involved in DNA synthesis. Despite its importance in both replication fork assembly and progression, the precise role of Mcm10 remains undefined. In order to better understand the importance of the molecular interactions of vertebrate Mcm10, we have carried out a structure-function study of the protein from Xenopus laevis (XMcm10), which shares a high sequence homology with the human ortholog. XMcm10 contains three structured regions: a putative oligomerization domain at the N-terminus (NTD) and two independent DNA and pol α binding regions located in the internal (ID) and C-terminal (CTD) domains of the protein. We present a biochemical characterization of the individual domains in Chapter 2, followed by the three-dimensional solution NMR structure and DNA binding activity of the CTD in Chapter 3. The results reveal how the CTD zinc cluster binds DNA and suggests a putative role for this motif in protein-protein interactions with other replisome components. In addition, we show using XMcm10 constructs spanning the two DNA binding domains that the region between is flexible in solution, and that this linker is necessary for optimal DNA binding by XMcm10. Finally, preliminary structural evidence for how the individual ID and CTD modules coordinate DNA binding in the context of the full-length protein is presented in Chapter 4. This modular DNA binding strategy is discussed in terms of Mcm10’s role in during replication initiation and elongation. Advisors/Committee Members: Ellen H. Fanning (committee member), Brandt F. Eichman (committee member), Hassane Mchaourab (committee member), Walter J. Chazin (committee member), James G. Patton (Committee Chair).

Subjects/Keywords: DNA Replication; DNA Binding; Zinc Motif; Mcm10; NMR; C-Terminal Domain

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APA (6th Edition):

Robertson, P. D. (2010). Structural biology of the C-terminal domain of eukaryotic replication factor Mcm10. (Doctoral Dissertation). Vanderbilt University. Retrieved from http://hdl.handle.net/1803/12458

Chicago Manual of Style (16th Edition):

Robertson, Patrick David. “Structural biology of the C-terminal domain of eukaryotic replication factor Mcm10.” 2010. Doctoral Dissertation, Vanderbilt University. Accessed January 22, 2021. http://hdl.handle.net/1803/12458.

MLA Handbook (7th Edition):

Robertson, Patrick David. “Structural biology of the C-terminal domain of eukaryotic replication factor Mcm10.” 2010. Web. 22 Jan 2021.

Vancouver:

Robertson PD. Structural biology of the C-terminal domain of eukaryotic replication factor Mcm10. [Internet] [Doctoral dissertation]. Vanderbilt University; 2010. [cited 2021 Jan 22]. Available from: http://hdl.handle.net/1803/12458.

Council of Science Editors:

Robertson PD. Structural biology of the C-terminal domain of eukaryotic replication factor Mcm10. [Doctoral Dissertation]. Vanderbilt University; 2010. Available from: http://hdl.handle.net/1803/12458

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