Presentation Title

Septin modifying proteins in Candida albicans

Advisor Information

Jill Blankenship

Location

Dr. C.C. and Mabel L. Criss Library

Presentation Type

Poster

Start Date

4-3-2016 9:00 AM

End Date

4-3-2016 10:30 AM

Abstract

Septins are conserved, GTP-binding proteins important for cytokinesis, membrane compartmentalization, and exocytosis in eukaryotic cells. Their dynamic organization is maintained from yeast to mammals. In the fungus, Candida albicans, these proteins are necessary for its morphogenesis and pathogenicity; they regulate the fungus from rounded budding yeast to elongated hyphae – its filamentous cells. While septins are crucial for the pathogen’s virulence, very little is understood about the mechanisms by which septin structures are controlled. By testing a library of twelve mutant strains and growing them exponentially at 30°C, I was able to integrate a plasmid DNA previously digested from E. coli into the mutant strains. This new insertion created a modified mutant strain from which septin localization in filamentous cells and cell wall stress could be observed. Positive PCR (polymerase chain reaction) results suggested the insert was correctly integrated into the mutant strains. Septin genes known for filamentation and/or linked to cell wall integrity were previously tagged with GFP in order to visually observe septin localization in a microscope during these processes.

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COinS
 
Mar 4th, 9:00 AM Mar 4th, 10:30 AM

Septin modifying proteins in Candida albicans

Dr. C.C. and Mabel L. Criss Library

Septins are conserved, GTP-binding proteins important for cytokinesis, membrane compartmentalization, and exocytosis in eukaryotic cells. Their dynamic organization is maintained from yeast to mammals. In the fungus, Candida albicans, these proteins are necessary for its morphogenesis and pathogenicity; they regulate the fungus from rounded budding yeast to elongated hyphae – its filamentous cells. While septins are crucial for the pathogen’s virulence, very little is understood about the mechanisms by which septin structures are controlled. By testing a library of twelve mutant strains and growing them exponentially at 30°C, I was able to integrate a plasmid DNA previously digested from E. coli into the mutant strains. This new insertion created a modified mutant strain from which septin localization in filamentous cells and cell wall stress could be observed. Positive PCR (polymerase chain reaction) results suggested the insert was correctly integrated into the mutant strains. Septin genes known for filamentation and/or linked to cell wall integrity were previously tagged with GFP in order to visually observe septin localization in a microscope during these processes.