Date of Graduation
Master of Science in Cell and Molecular Biology
Thd2, histone deacetylase, inositol polyphosphate kinase, DNA damage, Tetrahymena thermophila
Medical Molecular Biology
The packaging of chromatin plays a large role in the ability of genes to either be accessible to transcription or inaccessible based on its level of acetylation. Specific enzymes such as histone acetyltransferases (HATs) add or histone deacetylases (HDACs) remove acetyl groups from histone proteins. Tetrahymena thermophila is ideal for the study of chromatin packaging because they contain two distinct nuclei, a macronucleus and a micronucleus, in which acetylation and transcription are drastically different. Thd2 is a class II HDAC that has been identified to function in the deacetylation of chromatin in the micronucleus. The other factors that interact with Thd2 and are required for deacetylation of the micronuclear chromatin are unknown. Thd2 has recently been shown to interact with malate dehydrogenase via immunoprecipitation and mass spectrometry. A thd2 knockout, which was found to be resistant to UV but not other forms of DNA damage, which may implicate a role in nucleotide excision repair specifically. THD2 also has two splice variants, Thd2a and Thd2b. The predominant form, Thd2a, has an inositol polyphosphate kinase (IPK) domain but further studies must be done to determine a role for this domain.
© Kailey Deane Barron
Barron, Kailey Deane, "Characterizing the Role of Tetrahymena Histone Deacetylase 2 in DNA Damage Repair in the Ciliate Tetrahymena Thermophila" (2012). MSU Graduate Theses. 1856.