Abstract
The yeast phosphatidylcholine/phosphatidylinositol transfer protein Sec14p is indispensable for vesicular transport from the Golgi and cell viability. The essential nature of Sec14p function can be bypassed by inactivation of other genes. These include enzymes in the CDP-choline pathway for phosphatidylcholine biosynthesis and the yeast oxysterol binding protein homologue Kes1p/Osh4p. To further understand the mechanism of sec14 bypass we performed a series of synthetic lethal analyses with each of approximately 4800 single deletion mutants. The results indicate ~ 31 genes required for the viability of the sec14 cki1 strain. Included within the 31 genes were components of the TRAPPII complex and ypt31 but not the closely related ypt32. In addition, these genes are not required for the viability of the sec14 kes1 strain, demonstrating a specific requirement for this mode of bypass. Furthermore, inactivation of the KES1 gene ameliorated the growth defects associated with the sec14 cki1 synthetic lethal interactions with the TRAPPII components and ypt31. Together the results demonstrate the differences between the modes of sec14 bypass. As well the results suggest that Kes1p may function as an inhibitor of Ypt31p, the TRAPPII complex, or possibly a protein upstream of TRAPPII function. (Supported by the Canadian Institutes of Health Research and the Canada Research Chairs fund)
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
