Coco Simon (VI), Lauren Poprik (VI), Divya Subramanian (VI), Kate Marine (VI), Isabelle Chen (V), James Draper (IV), Aanvi Trivedi (IV)
Project Summary
Cells must copy their DNA to grow and divide. DNA replication begins when a small region of the DNA double helix is unwound to expose single strands of DNA. A helicase protein is then shepherded onto the unwound DNA regions by other proteins known as loaders. Once loaded, the helicase can unwind long stretches of the chromosome in which the DNA is packaged, producing the template required by the replication machinery to duplicate the DNA. This process must be accurately executed to avoid generating errors that could damage the DNA and potentially cause cells to die.
DnaI is a helicase loader protein found in some types of bacteria. In the disease-causing bacterial species Staphylococcus aureus (S. aureus), an inhibitor protein from a virus that infects the bacteria, can interact with DnaI and halt S. aureus DNA replication, leading to cell death. However, how this viral protein controls the activity of the loader molecules has yet to be understood.” Hood, I. V. and Berger, JM. eLife. 2016
Project Goals
The Pathogens IRT group is working on performing experiments to confirm the interaction between the antibacterial viral protein (77ORF104) and its host target protein S. aureus DnaI helicase loader. Future investigations will further confirm the mechanism by which this antibacterial protein inhibits DNA replication, thereby killing the Gram-positive pathogen Staphylococcus aureus, which is one of the most common hospital-acquired infections.
Works Cited
Iris V Hood, James M Berger (2016). Viral hijacking of a replicative helicase loader and its implications for helicase loading control and phage replication eLife 5:e14158.
Faculty Advisor
Dr. Hood
