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Phospholipid synthesis and zinc transport in yeast
Author(s) -
Han GilSoo,
Walker Joel,
Eide David J.,
Carman George M.
Publication year - 2006
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.20.5.a947-a
Subject(s) - mutant , phospholipid , zinc , biochemistry , wild type , enzyme , chemistry , methyltransferase , saccharomyces cerevisiae , yeast , biology , microbiology and biotechnology , membrane , gene , methylation , organic chemistry
Zinc depletion represses several phospholipid biosynthetic enzymes including PE methyltransferase and phospholipid methyltransferase. These enzymes methylate PE to form PC. The high‐affinity plasma membrane zinc transporter Zrt1p plays a major role in regulating cellular levels of zinc. Given the fact that this transporter is localized within the membrane bilayer, its function might be governed by changes in phospholipid composition. To address this question, zinc uptake was measured in mutants (i.e., cho2 Δ opi3 Δ, and cho2 Δ opi3 Δ) defective in the phospholipid methyltransferase enzymes. These mutants were chosen to exacerbate the repressive effects that zinc depletion has on these enzymes. Zrt1pwas expressed in the mutant cells from a multicopy plasmid bearing the ZRT1 gene with a constitutive promoter. Zinc uptake was reduced in the cho2 Δ, opi3 Δ, and cho2 Δ opi3 Δ mutants by 43%, 20%, and 78%, respectively, when compared with wild type cells. The labile zinc pool was reduced in cho2 Δ and cho2 Δ opi3 Δ mutant cells by 4.5‐fold and 11‐fold, respectively, when compared with that of wild type cells. The labile zinc pool was not affected in the opi3 Δ mutant. Supported by NIH grant GM 28140.