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Western University

2012

Phosphorylation

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Full-Text Articles in Life Sciences

Characterization Of A Negative Regulatory Domain In Fushi Tarazu, A Pair-Rule Protein In Drosophila Melanogaster, Elyse Susanne Burlingham Aug 2012

Characterization Of A Negative Regulatory Domain In Fushi Tarazu, A Pair-Rule Protein In Drosophila Melanogaster, Elyse Susanne Burlingham

Electronic Thesis and Dissertation Repository

Fushi tarazu (FTZ) is a pair-rule protein important for the development of the anterior-posterior axis during embryogenesis. Low level ectopic expression of FTZΔ148-206 from a Tubulin α1 promoter, but not FTZ1-410 (full length FTZ), results in the anti-ftz phenotype in developing Drosophila melanogaster larvae, indicating that FTZΔ148-206 is a hyperactive FTZ protein. Through deletion analysis, using a high level ectopic expression system and assaying survivorship, I narrowed the location of the negative regulatory domain (NRD) to the 178-206 amino acid region of FTZ. Mutations that mimic both constitutive phosphorylation and dephosphorylation in the …


Phenotypic Analysis Of Schizosaccharomyces Pombe Strains Bearing Site-Directed Mutations In The Carboxy Terminal Domain Of The Largest Subunit Of Rna Polymerase Ii, Kyle S. Hoffman Aug 2012

Phenotypic Analysis Of Schizosaccharomyces Pombe Strains Bearing Site-Directed Mutations In The Carboxy Terminal Domain Of The Largest Subunit Of Rna Polymerase Ii, Kyle S. Hoffman

Electronic Thesis and Dissertation Repository

The phosphorylation status of the largest sub-unit of RNA polymerase II (Rpb1p) is crucial to the control of transcription in eukaryotes. The domain subject to this phosphorylation is known as the carboxyl terminal domain (CTD) and consists of multiple repeats (from 20 to 52 copies depending on the species in question) of the heptad sequence Y1S2P3T4S5P6S7. Interestingly, differential phosphorylation of S2, S5, and S7 residues is known to play an important role in the control of pre-mRNA processing. To determine the number …


Changes In The Mitochondrial Phosphoproteome During Mammalian Hibernation, Dillon J. Chung Jul 2012

Changes In The Mitochondrial Phosphoproteome During Mammalian Hibernation, Dillon J. Chung

Electronic Thesis and Dissertation Repository

Hibernation in mammals involves a suppression of metabolic rate thereby conserving energy. Many hibernation studies focus on the mitochondria due to their energy-producing role. I hypothesized that this pattern of rapid suppression of liver mitochondrial metabolism with gradual reversal, was related to changes in the phosphorylation state of Ictidomys tridecemlineatus’ mitochondrial proteins in different stages of torpor bouts. Phosphorylation of threonine and serine amino-acid residues (unique to 49, 41 and 47, 38 kDa proteins respectively), detected using immunoblotting, changes seasonally (threonine: summer active > winter, serine: summer active > torpor), whereas no seasonal difference was observed in phosphotyrosine residues. Changes in …