Copyright © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
February 09, 2015
Very Important Paper: Establishing the Stability and Reversibility of Protein Pyrophosphorylation with Synthetic Peptides
Lisa M. Yates and Dorothea Fiedler*
Key factors in elucidating the biological relevance of novel post-translational modifications are to understand their chemical and biochemical stability as well as their reversibility in a cellular context. To evaluate these factors for protein pyrophosphorylation (a currently poorly characterized modification) Yates and Fiedler (Princeton University) used a series of synthetic pyrophosphopeptides to demonstrate that the pyrophosphate moiety is generally chemically inert but can be rapidly removed by alkaline phosphatases in vitro. Most importantly, they observed enzyme-dependent depyrophosphorylation of the synthetic pyrophosphopeptides in mammalian and yeast cell lysates. These findings thus provide the initial evidence for the reversibility of pyrophosphorylation and highlight the potential impact of this modification on cellular signaling networks.
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