AI Article Synopsis
- Gpr1 protein in Yarrowia lipolytica is part of a little-studied protein family typically found in simpler organisms, and mutations in its gene lead to increased sensitivity to acetic acid at low pH levels.
- Numerous mutations in related GPR1 genes from another yeast, Saccharomyces cerevisiae, also cause similar hypersensitivity to acetic acid, highlighting the functional importance of specific protein regions.
- The phosphorylation of Gpr1p in Yarrowia lipolytica is influenced by these mutations, and research suggests that Gpr1p may exist as part of a larger protein complex.
Article Abstract
The Gpr1 protein of the ascomycetous yeast Yarrowia lipolytica belongs to the poorly characterized Gpr1/Fun34/YaaH protein family, members of which have thus far only been found in prokaryotes and lower eukaryotes. Trans-dominant mutations in the GPR1 gene result in acetic acid sensitivity of cells at low pH. Moreover, Gpr1p is subjected to phosphorylation at serine-37 in a carbon source-dependent manner. Here we show that several mutations within the ORFs of the GPR1 orthologues of Saccharomyces cerevisiae, YCR010c (ATO1) and YNR002c (ATO2), also trans-dominantly induce acetic acid hypersensitivity in this yeast. We demonstrate that the C-termini of mutated Gpr1p, Ycr010cp and Ynr002cp are necessary for the triggering of acetic acid sensitivity. Phosphorylation of Y. lipolytica Gpr1p was also affected by several mutations. Data further suggest that Gpr1p exists in an oligomeric state.
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| http://dx.doi.org/10.1111/j.1567-1364.2006.00191.x | DOI Listing |
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