Date of Award
7-17-2009
Degree Type
Thesis
Degree Name
Master of Science (MS)
Department
Chemistry
First Advisor
Dr. Yujun G. Zheng - Chair
Second Advisor
Dr. Giovanni Gadda
Third Advisor
Dr. Aimin Liu
Abstract
Tip60 is a 60 kDa nuclear protein which exists in three isoforms, belongs to the MYST/HAT family of proteins and was discovered after its interaction with the Human HIV-1 Tat. As a nuclear protein, Tip60 can act as a coactivator or repressor. To understand the HAT action of Tip60, two possible catalytic models exist; the ping-pong and the ternary complex formation models. In correlation with the exploration of HAT catalytic action, mutations of a Cys to Ala and a Glu to Gln on Esa1 (yeast homolog of Tip60 and MYST/HAT prototype), was reported to show wild type-like and decreased acetylating properties, respectively. In this work, Tip60 HAT action was explored. In Tip60, the Cys in the active site is important for acetylation of the H4(1-20) substrate and the Glu showed semi loss in acetylating the H4(1-20) peptide substrate. These data highlight a unique mechanism of Tip60 catalysis.
DOI
https://doi.org/10.57709/1059242
Recommended Citation
Elangwe, Emilia N., "Site Directed Mutagenesis, Expression and Enzymatic Studies of the 60 kDa Human HIV-TAT 1 Interactive Protein, TIP60." Thesis, Georgia State University, 2009.
doi: https://doi.org/10.57709/1059242