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Intern: Scott Montgomery, University of Washington Mentor: Martin Sagermann Faculty Supervisor: Martin Sagermann Department: Chemistry and Biochemistry

PURIFICATION OF A TRUNCATED H-SUBUNIT OF VMA13P, A V-TYPE ATPASE

The V-type ATPases use ATP to actively transport protons into organelles and extracellular compartments. The H-subunit, or Vma13p, is a 478 amino acid protein that plays an essential regulatory role in V-type ATPase activity. Previous crystallization studies of the Saccharomyces cerevisiae H-subunit have revealed potential binding regions for the ATPase and other macromolecules. In this study, a truncated version of the H-subunit, lacking the C-terminal domain, has been recombinantly overexpressed in Escherichia coli and purified. The subunit is currently undergoing crystallization trials using the hanging-drop vapor-diffusion method. Additionally, preliminary yeast pull down experiments using both the wild type and truncated subunits suggest a number of potential proteins that may interact with the H-subunit, including other V-type ATPase proteins.

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