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Stander Symposium abstract book - University of Dayton

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POSTER SESSION 1<br />

plicate genes bab1 and bab2 that encode the Bab1 and Bab2 transcription factor proteins. These proteins block pigment development as they<br />

repress the expression <strong>of</strong> genes needed for the pigment metabolic pathway. For Drosophila melanogaster, the dorsal cuticle covering the posterior<br />

abdominal segments <strong>of</strong> males, but not females, is fully pigmented. This sexual dimorphism stems from the absence <strong>of</strong> Bab1 and Bab2 expression<br />

from these segments in males. Interestingly though, females from different geographic populations vary in the extent <strong>of</strong> pigmentation ranging<br />

from a near total absence to a more male-like pattern. I hypothesized that differences in Bab1 and Bab2 expression would exist between females<br />

with different extents <strong>of</strong> abdominal pigmentation. For my thesis I have employed in situ hybridization and immunohistochemical methods to test<br />

this hypothesis through observations <strong>of</strong> the mRNA and protein products respectively. My results raise new questions regarding how the expression<br />

patterns <strong>of</strong> duplicate genes evolve.<br />

Do Trends in Bacterial Replication Restart Pathways Depend on the Presence <strong>of</strong><br />

Primosome Protein DnaT?<br />

Presenter(s): Linda Berg<br />

Advisor(s): Matthew E Lopper<br />

Chemistry - Graduate Research<br />

Throughout the life <strong>of</strong> a cell, the process <strong>of</strong> DNA replication is challenged by factors that can bring about damage to the DNA, which ultimately<br />

leads to a halt in DNA replication and, if not corrected, cell death. Bacteria solve this problem with a mechanism called DNA replication restart. DNA<br />

replication restart is catalyzed by primosome proteins which are well-studied in the model organism, E. coli. However, not all bacteria encode the<br />

full complement <strong>of</strong> primosome proteins, suggesting that differences might exist in DNA replication restart pathways among diverse bacteria. N.<br />

gonorrhoeae, for example, lacks a DnaT homolog, but DnaT is encoded by E. coli and is thought to affect interactions between primosome protein<br />

PriB and single-stranded DNA. This raises the question <strong>of</strong> how a bacterium might compensate for lack <strong>of</strong> a primosome protein, such as DnaT, that<br />

provides otherwise essential functions in some bacteria. Since N. gonorrhoeae PriB has a weak interaction with single-stranded DNA, as opposed<br />

to the strong interaction between PriB and single-stranded DNA in E. coli, we hypothesized that the presence <strong>of</strong> a DnaT homolog could be used<br />

to predict the affinity with which a bacterial PriB would bind single-stranded DNA. Binary interactions between PriB and single-stranded DNA <strong>of</strong><br />

two bacteria, Klebsiella pneumoniae (which encodes a DnaT homolog) and Yersinia enterocolitica (which lacks a DnaT homolog) were analyzed.<br />

Both K. pneumoniae and Y. enterocolitica have a high affinity PriB:single-stranded DNA interaction with dissociation constants <strong>of</strong> ~62 nM and<br />

~84 nM, respectively. Thus, the presence <strong>of</strong> DnaT cannot be used to predict affinities <strong>of</strong> binary interactions between PriB and single-stranded DNA.<br />

However, the experimentally measured binding constants combined with amino acid sequence alignments <strong>of</strong> the PriB homologs have led to the<br />

definition <strong>of</strong> parameters for high affinity binary interactions between PriB and single-stranded DNA.<br />

Inhibition <strong>of</strong> the PriA and PriB Primosome Proteins <strong>of</strong> the Neisseria gonorrhoeae<br />

Replication Restart Pathway.<br />

Presenter(s): Hayley E Ward<br />

Advisor(s): Matthew E Lopper<br />

Chemistry - Honors Thesis<br />

DNA damage that occurs in bacterial cell DNA can lead to cell death by inhibiting the replication <strong>of</strong> genetic material. Bacteria, such as Neisseria<br />

gonorrhoeae, have developed a method to avoid cell death due to premature termination <strong>of</strong> DNA replication using a DNA replication restart pathway.<br />

Previous research has determined that there are two proteins, PriA and PriB, that play an important roll in the replication restart pathway.<br />

Collectively, these enzymes bind to the DNA and facilitate reloading <strong>of</strong> the replication machinery in order to initiate replication without an origin<br />

sequence. The proposed study will look for possible inhibitors to the function <strong>of</strong> PriA and PriB and will also explore the method through which<br />

these inhibitors function. These inhibitors could potentially be developed into novel antibiotics against N. gonorrhoeae.<br />

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