We investigate a family of proteins called pentapeptide repeat proteins in attempt to solve their structures and functions within cyanobacteria. We attempt to solve protein structures through protein X-ray crystallography and attempt to solve the function of our proteins through various methods including generating growth curves, filament length distributions, monitoring heterocyst formation frequencies and patterns, localizing the protein within cyanobacteria, rtPCR experiments and binding partner assays. Essentially the question we have asked is, what are these proteins that are over-abundant in cyanobacteria specifically, doing in cells and is it related to the nitrogen fixation or cell differentiation processes that cyanobacteria carry out. These questions are critical to the fields of environmental science where we need to understand and prevent cyanobacteria from continuing to cause algal blooms that destroy ecosystems across the nation. It can also have some strong medical implications if any pentapeptide repeat proteins are found to impact the cells ability to differentiate or regulate its cell cycle. The major findings of our study are that increased expression of our protein has been demonstrated to correlate with increased growth of cyanobacteria strains in a step-wise fashion. This could indicate that our protein may have some role in helping the cyanobacteria survive in stressful environments or that it may have regulatory function. Determining the mechanism by which our protein positively correlates with cell growth is our next step. This experience has been incredibly relevant for my intended career in medicine by teaching me both leadership and analytical skills help me not only understand research at a deeper level but also lead a team of peers.
Author: Andrew Bellas
Advisor: Michael Kennedy, Chemistry and Biochemistry
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