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Characterization of Gylcerophosphocholine Acyltransferase Homolog, Gpc1, in Candida albicans
Author(s) -
King William Ray,
PattonVogt Jana
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.796.6
Subject(s) - candida albicans , acyltransferase , biochemistry , phospholipid , biosynthesis , phosphatidylcholine , acyltransferases , chemistry , saccharomyces cerevisiae , biology , microbiology and biotechnology , gene , membrane
The maintenance of membrane composition through regulated synthesis and turnover of phospholipids is crucial to cellular homeostasis. Phosphatidylcholine (PC) is the most abundant phospholipid in most eukaryotic membranes. We have identified a glycerophosphosphocholine acyltransferase (GPCAT), Gpc1, that expands our understanding of PC biosynthesis and acyl chain remodeling in Saccharomyces cerevisiae . Gpc1 acylates glycerophosphocholine (GPC), a product of complete deacylation of PC, to form lysophosphotidylcholine (LysoPC). LysoPC can subsequently be converted to PC by Ale1. This PC deacylation reacylation pathway (PC‐DRP) defines a novel route for PC biosynthesis and provides a potential mechanism to alter the acyl chain composition of a PC molecule. Changes in acyl chain composition can, in turn, affect physical properties of a membrane, such as fluidity, width, thickness and shape. Gpc1 displays no homology to known acyltransferases and defines a new gene family with members in animals, plants and fungi. The pathogenic fungus Candida albicans displays robust transport of GPC into the cell. We have previously shown that the inability of C. albicans to transport GPC results in decreased virulence in a mouse model of disseminated candidiasis implying this metabolite may play an important role during pathogenicity. Here we report on the creation of a C. albicans diploid knockout of Gpc1 homolog (orf19.998) using a transient CRISPR Cas‐9 system. Radiolabeling coupled with mass spectrometry are being employed to determine if the caGpc1 is similar to the scGpc1 in terms of biochemical function. Initial studies to examine the physiological role of caGpc1 are being performed. Support or Funding Information NIH R15GM104876 (to JPV) This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .