Event Title
Investigating the Mechanism of Tup1 Regulation of Candida albicans Filamentation
Presentation Type
Poster/Portfolio
Presenter Major(s)
Cell and Molecular Biology
Mentor Information
Derek Thomas
Department
Biomedical Sciences
Location
Henry Hall Atrium 67
Start Date
10-4-2013 11:00 AM
End Date
10-4-2013 12:00 PM
Keywords
Life Science
Abstract
Candidiasis is the fourth most prevalent nosocomial infection both in the US and worldwide. Unfortunately these infections carry unacceptably high morbidity and mortality rates. C. albicans is a diploid fungus that has the ability to grow as a blastopore, pseudo-hyphae, and hyphae. The ability to transition between the yeast and hyphal forms appears to be a key virulence trait for C. albicans. Tup1 plays a role early in the filamentation process and has been shown to be phosphorylated. It appears this phosphorylation is linked to the regulation of filamentation. Tup1 acts with the DNA binding proteins Nrg1 and Rfg1 as a transcriptional regulator to repress the expression of hyphal specific genes. An His-tagged version of Tup1 was purified using nickel-NTA columns and analyzed using LC MS/MS using CID and ETD to identify sites of phosphorylation. This strain was also used to facilitate Co-IP to define the groups of proteins interacting with Tup1.
Investigating the Mechanism of Tup1 Regulation of Candida albicans Filamentation
Henry Hall Atrium 67
Candidiasis is the fourth most prevalent nosocomial infection both in the US and worldwide. Unfortunately these infections carry unacceptably high morbidity and mortality rates. C. albicans is a diploid fungus that has the ability to grow as a blastopore, pseudo-hyphae, and hyphae. The ability to transition between the yeast and hyphal forms appears to be a key virulence trait for C. albicans. Tup1 plays a role early in the filamentation process and has been shown to be phosphorylated. It appears this phosphorylation is linked to the regulation of filamentation. Tup1 acts with the DNA binding proteins Nrg1 and Rfg1 as a transcriptional regulator to repress the expression of hyphal specific genes. An His-tagged version of Tup1 was purified using nickel-NTA columns and analyzed using LC MS/MS using CID and ETD to identify sites of phosphorylation. This strain was also used to facilitate Co-IP to define the groups of proteins interacting with Tup1.