Julie Wolf

E-mail: wolfx202@umn.edu

Thesis Advisor: Dana Davis

Year entered: 2004

Degrees received:
B.S., Microbiology, University of Michigan, Ann Arbor, MI

Thesis research:
Candida albicans is the primary cause of fungal disease in humans.  This fungus is able to colonize and grow in tissue at a wide range of pH.  The protein Snf7 has been demonstrated to be necessary for C. albicans response to a neutral/alkaline environment as well as required for proper endosomal trafficking.  Thus characterization of Snf7 will increase understanding of two important processes within this human pathogen.  C. albicans growth in a neutral-alkaline environment requires processing of Rim101, a zinc-finger transcription factor.  At alkaline pH, Rim101 is processed from a full-length, inactive form (85 kDa) to a truncated form (74 kDa).  Rim101 processing is controlled through a signal transduction pathway, which includes the recently identified member, Snf7.  Snf7 also functions in the endosomal sorting complex required for transport (ESCRT) pathway.  The ESCRT pathway is important in promoting multivesicular body (MVB) formation and subsequent endosome-to-vacuole fusion.  In a large-scale yeast two-hybrid screen, Saccharomyces cerevisiae Snf7 was shown to interact with both Rim101 pathway members and ESCRT pathways members.  Additionally, some ESCRT pathway proteins are required for Rim101 processing to occur, although Rim101 processing is not necessary for endosome-to-vacuole fusion.  Based on this information,I hypothesize thatCandida albicans Snf7 can interact with both the ESCRT pathway proteins and the Rim101 processing proteins; that both interactions are localized to the endosomal membrane; and that these functions are distinct and separable.