Yeast PH Domains: A Study in Phosphoinositide Binding

Author

Heather Leigh Eisler, Utah State University

Date of Award:

5-1-2002

Document Type:

Thesis

Degree Name:

Master of Science (MS)

Department:

Biology

Committee Chair(s)

Daryll B. DeWald

Committee

Daryll B. DeWald

Committee

Lance C. Seefeldt

Committee

Gregory J. Podgorski

Abstract

Phosphoinositides are membrane-associated phospholipids whose inositol head group can be reversibly phosphorylated. PH domains are known to bind phosphoinositides. Yeast PH domains YPR091C and YNL144C were examined for their phosphoinositide binding using two different assays. The YPR091C PH domain bound specifically to PtdIns(4)P and PtdIns(5)P. The YNL144C PH domain did not bind to any phosphoinositide. The absence and the over expression of the YPR091C and YNL144C genes was studied in the yeast. The ypr091^CΔ strain grew slower at 37°C. The ynl144^CΔ yeast strain showed no growth defect at 37°C, higher salt concentrations, or when transformed with either the pYES2 plasmid or the pYES2 plasmid containing the YNL144C PH domain and grown on galactose media. Over expression of the YPR091C PH domain, in a strain that contained a wild type version of the gene, caused the strain to grow faster than the control at higher temperatures.

Recommended Citation

Eisler, Heather Leigh, "Yeast PH Domains: A Study in Phosphoinositide Binding" (2002). Biology. 687.
https://digitalcommons.usu.edu/etd_biology/687