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You searched for +publisher:"Penn State University" +contributor:("Jerry L Workman, Committee Chair/Co-Chair"). Showing records 1 – 3 of 3 total matches.

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Penn State University

1. Shia, Wei-Jong. FUNCTIONAL CHARACTERIZATION OF THE SAS (SOMETHING ABOUT SILENCING) COMPLEX IN BUDDING YEAST SACCHAROMYCES CEREVISIAE.

Degree: 2008, Penn State University

The yeast SAS2 (Something About Silencing 2) gene encodes a member of MYST (hMOZ, yYbf2/Sas3, ySas2, and dTIP60) family of histone acetyltransferases (HATs) and is involved in transcriptional silencing at all silent loci (HML, HMR, telomeres, and rDNA) in Saccharomyces cerevisiae. Here we show that the native SAS complex is a trimeric protein complex composed solely of Sas2, Sas4, and Sas5. The SAS complex is capable of acetylating core histones and nucleosomes through its catalytic subunit Sas2. The conserved MYST domain in Sas2 is essential for both the silencing function and histone acetyltransferase activity of the SAS complex. More importantly, SAS exclusively acetylates lysine 16 of histone H4, and this specific lysine preference corresponds to the role of SAS complex in antagonizing the spreading of Sir proteins at chromosome ends. In addition to the SAS complex, histone variant H2A.Z also plays an important role in anti-silencing function at subtelomeric regions. We demonstrate that SAS2 and HTZ1 synergistically regulate a subset of genes near telomeres for transcription activation. In the absence of SAS2, H4 lysine 16 acetylation and H2A.Z are both reduced at subtelomeric regions. Furthermore, mutation at H4 lysine 16 causes the same H2A.Z loss. When recruited, SAS enhances the H4 lysine 16 acetylation and the subsequent H2A.Z enrichment. Our data suggest that acetylation of H4 lysine 16 by SAS is required for incorporation of H2A.Z near telomeres. As a result, the presence of H4 lysine 16 acetylation and H2A.Z thus synergistically prevents the ectopic propagation of heterochromatin. Advisors/Committee Members: Jerry L Workman, Committee Chair/Co-Chair, Joseph C. Reese, Committee Chair/Co-Chair, David Scott Gilmour, Committee Member, Hong Ma, Committee Member, Song Tan, Committee Member.

Subjects/Keywords: SAS; H2A.Z; anti-silencing; HAT

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Shia, W. (2008). FUNCTIONAL CHARACTERIZATION OF THE SAS (SOMETHING ABOUT SILENCING) COMPLEX IN BUDDING YEAST SACCHAROMYCES CEREVISIAE. (Thesis). Penn State University. Retrieved from https://submit-etda.libraries.psu.edu/catalog/7080

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Shia, Wei-Jong. “FUNCTIONAL CHARACTERIZATION OF THE SAS (SOMETHING ABOUT SILENCING) COMPLEX IN BUDDING YEAST SACCHAROMYCES CEREVISIAE.” 2008. Thesis, Penn State University. Accessed April 13, 2021. https://submit-etda.libraries.psu.edu/catalog/7080.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Shia, Wei-Jong. “FUNCTIONAL CHARACTERIZATION OF THE SAS (SOMETHING ABOUT SILENCING) COMPLEX IN BUDDING YEAST SACCHAROMYCES CEREVISIAE.” 2008. Web. 13 Apr 2021.

Vancouver:

Shia W. FUNCTIONAL CHARACTERIZATION OF THE SAS (SOMETHING ABOUT SILENCING) COMPLEX IN BUDDING YEAST SACCHAROMYCES CEREVISIAE. [Internet] [Thesis]. Penn State University; 2008. [cited 2021 Apr 13]. Available from: https://submit-etda.libraries.psu.edu/catalog/7080.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Shia W. FUNCTIONAL CHARACTERIZATION OF THE SAS (SOMETHING ABOUT SILENCING) COMPLEX IN BUDDING YEAST SACCHAROMYCES CEREVISIAE. [Thesis]. Penn State University; 2008. Available from: https://submit-etda.libraries.psu.edu/catalog/7080

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


Penn State University

2. Guelman, Sebastian. CHARACTERIZATION OF TWO DISTINCT dGCN5-CONTAINING HAT COMPLEXES IN DROSOPHILA .

Degree: 2008, Penn State University

Eukaryotes organize their genomes in the form of chromatin, a filament composed of DNA, histones and non-histone proteins. Chromatin structure plays crucial roles in the regulation of nuclear processes that employ DNA as template, including transcription, DNA replication, repair and recombination. Chromatin structure can be altered to allow such processes to occur in the cell. One way to do so is by covalently modifying different amino acid residues present at the histone N-terminal tails, which protrude away from the nucleosomes. These modifications can affect inter-nucleosomal interactions and result in changes in the compaction of chromatin. In addition, covalently modified histone tails can recruit additional factors which can trigger downstream events. Acetylation is one of the best characterized histone modifications. This modification is performed by histone acetyltransferases (HATs), which transfer an acetyl group from acetyl CoA to lysine residues of the histone tails. This modification is reversible and can be removed by histone deacetylases. The yeast coactivator SAGA provides a good example of a HAT and has been studied in detail. Different experiments demonstrated that histone acetylation by the SAGA complex is required for transcription of a subset of genes. Gcn5 is the catalytic subunit of this complex and is highly conserved throughout eukaryotes. At the time we began this project, the dGcn5 (Drosophila Gcn5) gene had been cloned but no additional information was available about dGcn5. Therefore, we sought to determine if dGcn5 forms part of multi-subunit protein complexes in flies, which would enable us to understand the role of dGcn5 in fly development. This thesis describes the purification of dGcn5 as part of two distinct HAT complexes. One of these complexes is dSAGA (Drosophila SAGA), which shares homologous subunits with yeast SAGA and the mammalian complexes STAGA, PCAF and TFTC. We identified a novel WD-repeat containing protein in dSAGA and demonstrated that this protein is essential for viability and required for histone H3 acetylation in the embryo. The other dGcn5-containing complex we purified, ATAC (Ada Two A Containing), harbors an orthologue of the human VP16-interacting protein HCF-1, as well as other uncharacterized proteins with conserved domains. ATAC is very different from SAGA, both in size and biochemical composition, which suggests that ATAC and dSAGA carry out distinct functions during Drosophila development Advisors/Committee Members: Jerry L Workman, Committee Chair/Co-Chair, Susan M. Abmayr, Committee Member, Song Tan, Committee Member, Richard W Ordway, Committee Member, David Scott Gilmour, Committee Chair/Co-Chair.

Subjects/Keywords: histone; HAT; ATAC; dSAGA; Gcn5; Chromatin; Drosophila

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Guelman, S. (2008). CHARACTERIZATION OF TWO DISTINCT dGCN5-CONTAINING HAT COMPLEXES IN DROSOPHILA . (Thesis). Penn State University. Retrieved from https://submit-etda.libraries.psu.edu/catalog/6696

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Guelman, Sebastian. “CHARACTERIZATION OF TWO DISTINCT dGCN5-CONTAINING HAT COMPLEXES IN DROSOPHILA .” 2008. Thesis, Penn State University. Accessed April 13, 2021. https://submit-etda.libraries.psu.edu/catalog/6696.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Guelman, Sebastian. “CHARACTERIZATION OF TWO DISTINCT dGCN5-CONTAINING HAT COMPLEXES IN DROSOPHILA .” 2008. Web. 13 Apr 2021.

Vancouver:

Guelman S. CHARACTERIZATION OF TWO DISTINCT dGCN5-CONTAINING HAT COMPLEXES IN DROSOPHILA . [Internet] [Thesis]. Penn State University; 2008. [cited 2021 Apr 13]. Available from: https://submit-etda.libraries.psu.edu/catalog/6696.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Guelman S. CHARACTERIZATION OF TWO DISTINCT dGCN5-CONTAINING HAT COMPLEXES IN DROSOPHILA . [Thesis]. Penn State University; 2008. Available from: https://submit-etda.libraries.psu.edu/catalog/6696

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


Penn State University

3. Chandy, Mark. HISTONE MODIFICATIONS INFLUENCE CHROMATIN MODIFYING AND CHROMATIN REMODELING COMPLEXES .

Degree: 2008, Penn State University

Chromatin condenses DNA and packages it into the nucleus. The fundamental unit of chromatin is the nucleosome, which compacts and forms higher order structures. Chromatin structure affects transcription, DNA replication and DNA repair. For gene expression, chromatin is dynamically modulated by chromatin modifying complexes and chromatin remodeling complexes. The histone code hypothesis predicts that modifications not only dictate the inheritance of chromatin states, but also that combinations of modifications recognized by protein-interaction domains are important for recruiting cofactors that alter chromatin structure. For over 40 years, histone acetylation has been associated with gene activation. Moreover, the discovery of histone acetyl transferase (HAT) complexes has implicated acetylation in transcription, DNA repair and even silencing. The SAGA complex is a 1.8 MDa multisubunit HAT complex that is recruited by activator at promoters. As the catalytic subunit of SAGA, Gcn5 acetylates promoter nucleosomes and produces a peaked acetylation profile upon gene induction. Moreover, the Gcn5 bromodomain is required for retention on acetylated nucleosomes. We test the importance of the Gcn5 bromodomain in restricting SAGA acetylation to the promoter using the scanning in vitro chromatin immunoprecipitation assay. The Gcn5 bromodomain does not significantly affect the nucleosomal acetylation profile of SAGA, even when the activator is removed from the array. While the Spt7 bromodomain does not retain SAGA on acetylated nucleosomes in vitro, its evolutionary conservation in yeast suggests that it may help retain SAGA on acetylated nucleosomes in vivo. When tested on phenotypic screens, the Spt7 bromodomain mutant and the Spt7 and Gcn5 double bromodomain mutant have a slight phenotype. The accumulation of acetylated histones at the promoter signals for the recruitment of other cofactors. SAGA and the ATP dependent chromatin remodeler, SWI/SNF functioned cooperatively in the activation of several genes in budding yeast. At the PHO5 promoter, both SAGA and SWI/SNF are important for timely removal of nucleosomes from the promoter. The loss of SWI/SNF results in the accumulation of H3K9 acetylated histones at this promoter, which is also an acetylation site for SAGA. Thus, SAGA acetylation at the promoter may recruit SWI/SNF and promote the displacement of acetylated nucleosomes. We directly test the influence of SAGA acetylation on SWI/SNF nucleosome displacement using several assays on the immobilized nucleosome array in vitro. SWI/SNF not only displaces acetylated nucleosomes, but it also targets promoter acetylated nucleosomes in the absence of activator. More important, SWI/SNF displacement of acetylated nucleosomes correlates with an increase in accessible DNA at the promoter. Advisors/Committee Members: James E Hopper, Committee Chair/Co-Chair, Sergei A Grigoryev, Committee Member, Michael G Fried, Committee Member, Laura Carrel, Committee Member, Jerry L Workman, Committee Chair/Co-Chair, Robert G Levenson, Committee Member.

Subjects/Keywords: SAGA; SWI/SNF; chromatin remodeling; bromodomain

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Chandy, M. (2008). HISTONE MODIFICATIONS INFLUENCE CHROMATIN MODIFYING AND CHROMATIN REMODELING COMPLEXES . (Thesis). Penn State University. Retrieved from https://submit-etda.libraries.psu.edu/catalog/6926

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Chandy, Mark. “HISTONE MODIFICATIONS INFLUENCE CHROMATIN MODIFYING AND CHROMATIN REMODELING COMPLEXES .” 2008. Thesis, Penn State University. Accessed April 13, 2021. https://submit-etda.libraries.psu.edu/catalog/6926.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Chandy, Mark. “HISTONE MODIFICATIONS INFLUENCE CHROMATIN MODIFYING AND CHROMATIN REMODELING COMPLEXES .” 2008. Web. 13 Apr 2021.

Vancouver:

Chandy M. HISTONE MODIFICATIONS INFLUENCE CHROMATIN MODIFYING AND CHROMATIN REMODELING COMPLEXES . [Internet] [Thesis]. Penn State University; 2008. [cited 2021 Apr 13]. Available from: https://submit-etda.libraries.psu.edu/catalog/6926.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Chandy M. HISTONE MODIFICATIONS INFLUENCE CHROMATIN MODIFYING AND CHROMATIN REMODELING COMPLEXES . [Thesis]. Penn State University; 2008. Available from: https://submit-etda.libraries.psu.edu/catalog/6926

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

.