AI Article Synopsis
- Gpr1 protein in Yarrowia lipolytica is part of a poorly understood protein family, and it plays a role in adapting to acetic acid at low pH.
- Phosphorylation of Gpr1p depends on the carbon source, with complete dephosphorylation occurring when the carbon source is exhausted and re-phosphorylation happening when a new source is added.
- Phosphorylation primarily occurs at serine-37, but there is no clear link between Gpr1p phosphorylation levels and the hypersensitivity to acetic acid related to Gpr1p mutations.
Article Abstract
The Gpr1 protein of the ascomycetous yeast Yarrowia lipolytica belongs to the poorly characterised Gpr1/Fun34/YaaH protein family whose members have been only found in prokaryotes and lower eukaryotes so far. Gpr1p seems to be involved in acetic acid adaptation at low pH values. Here we show that Gpr1p is subjected to phosphorylation in dependence on the carbon source. Exhaustion of the carbon source resulted in a complete dephosphorylation of Gpr1p, whereas addition of a new carbon source caused the phosphorylation of Gpr1p. Almost all Gpr1p molecules became phosphorylated after addition of acetate, while other carbon sources only triggered the phosphorylation of about half of the Gpr1p molecules. Phosphorylation was found to occur at serine-37. In spite of the clear effect of acetate/acetic acid on the level of phosphorylation of Gpr1p, no correlation of phosphorylation/dephosphorylation and acetic acid hypersensitivity, caused by mutations within Gpr1p, was detected.
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| http://dx.doi.org/10.1016/j.femsyr.2005.04.009 | DOI Listing |
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