Investigating the role of histone acetylation in yeast FACT complex function
department or school: Medicine, Faculty of
department or school: Biochemistry and Molecular Biology, Department of
data provider: DSpace
degree campus: UBCV
creator: Shimizu, Jed Chih-Leh
issued: 2010-01-14T00:29:41Z
issued: 2006
related degree: Master of Science - MSc
degree grantor: University of British Columbia
description: The FACT (facilitates chromatin transactions) complex, a heterodimer comprised of Spt l6p and Pob3p, is involved in a number of processes involving DNA, including transcription initiation, elongation, and repression, DNA replication, and DNA repair. FACT is thought to facilitate these processes through its ability to bind histones and reversibly alter nucleosomal structure modulating DNA accessibility. Recent data has shown that the Sptl6p subunit of FACT interacts with Sas3p of the NuA3 HAT (histone acetyl transferase) complex. Interestingly, mutants of NuA3 share none of the many phenotypes observed in FACT mutants, suggesting that this putative interaction may be redundant to other unknown FACT interactions. In the first part of this study, we confirmed the interaction between FACT and NuA3, and proceeded to describe, for the first time, an interaction between FACT and the ADA HAT complex both in vivo and in vitro. The interaction of FACT with NuA3 and ADA was then mapped to the Nterminal 482 residues of the Sptl6Δp FACT subunit. However, attempts to implicate this interaction with known FACT functions were unsuccessful. Biochemical approaches similarly failed to demonstrate a role for FACT in NuA3 and ADA complex function. The second part of this study focused on the novel spt16Δ922 mutant, which expresses 182 residues more of the Sptl6Δp polypeptide than the sptl6ΔNTD allele, yet possesses a number of mutant phenotypes. Our results show that the spt16Δ922 mutation causes a loss in histone H3 acetylation, supporting the hypothesis that the protein encoded by spt16Δ922 is interfering with normal histone interactions. This loss in histone acetylation was shown to parallel the generation of an spt phenotype, suggesting a possible role for histone acetylation in preventing aberrant transcription. However, further work examining the role of histone acetylation with respect to FACT yielded conflicting results. We conclude that spt16Δ922 is interfering with histone mod…
aggregated CHO: https://circle.library.ubc.ca/rest/handle/2429/18150
note: INVESTIGATING THE ROLE OF HISTONE ACETYLATION IN YEAST FACT COMPLEX FUNCTION by JED CHIH-LEH SHIMIZU B . S c , The University of British Columbia, 2003 A THESIS S U B M I T T E D I N P A R T I A L F U L F I L L M E N T OF T H E R E Q U I R E M E N T S F O R T H E D E G R E E OF M A S T E R OF S C I E N C E in T H E F A C U L T Y OF G R A D U A T E S T U D I E S (Biochemistry and Molecular Biology) T H E U N I V E R S I T Y OF BRIT ISH C O L U M B I A July 2006 © Jed Chih-Leh Shimizu, 2006 Abstract The F A C T (facilitates chromatin transactions) complex, a heterodimer comprised of Sptl6p and Pob3p, is involved in a number of processes involving D N A , including transcription initiation, elongation, and repression, D N A replication, and D N A repair. F A C T is thought to facilitate these processes through its ability to bind histones and reversibly alter nucleosomal structure modulating D N A accessibility. Recent data has shown that the Sptl6p subunit of F A C T interacts with Sas3p of the N u A 3 H A T (histone acetyl transferase) complex. Interestingly, mutants of N u A 3 share none of the many phenotypes observed in F A C T mutants, suggesting that this putative interaction may be redundant to other unknown F A C T interactions. In the first part of this study, we confirmed the interaction between F A C T and N u A 3 , and proceeded to describe, for the first time, an interaction between F A C T and the A D A H A T complex both in vivo and in vitro. The interaction of F A C T with N u A 3 and A D A was then mapped to the N -terminal 482 residues of the Sptl6p F A C T subunit. However, attempts to implicate this interaction with known F A C T functions were unsuccessful. Biochemical approaches similarly failed to demonstrate a role for F A C T in N u A 3 and A D A complex function. The second part of this study focused on the novel sptl6A922 mutant, which expresses 182 residues more of the Sptl6p polypeptide than the sptl6ANTD allele, yet possesses a number of …
has type: Thesis/Dissertation
date issued: 2006-11
is shown at: 10.14288/1.0092795
language: eng
degree discipline: Biochemistry and Molecular Biology
provider: Vancouver : University of British Columbia Library
publisher: University of British Columbia
rights: For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.
scholar level: Graduate
type: Text
identifier URI: http://hdl.handle.net/2429/18150