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.
Recently Published Articles
- Enhancing Antibody Response against Small Molecular Hapten with Tobacco Mosaic Virus as a Polyvalent Carrier
Xia Zhao, Limin Chen, Jittima Amie Luckanagul, Xiaolei Zhang, Yuan Lin and Qian Wang
Accepted manuscript online: 24 APR 2015 06:21AM EST | DOI: 10.1002/cbic.201500028
- Activity Fed Translation Assay "AFT", a new high throughput screening strategy for enzymes in droplets
Patrice Soumillion, Gabrielle Woronoff, Andrew Griffiths, Julia Wessel, Michael Ryckelynck and Olivier Schicke
Accepted manuscript online: 24 APR 2015 06:21AM EST | DOI: 10.1002/cbic.201500087
- Genetic Incorporation of Nε-formyllysine, a Novel Histone Posttranslational Modification
Tianyuan Wang, Qing Zhou, Fahui Li, Yang Yu, Xuebin Yin and Jiangyun Wang
Accepted manuscript online: 24 APR 2015 06:21AM EST | DOI: 10.1002/cbic.201500170
- Exploring Bacterial Heparinase II Activities with Defined Substrates
Lisa Bohlmann, Dr. Chih-Wei Chang, Prof. Ifor Beacham and Prof. Dr. Mark von Itzstein
Article first published online: 23 APR 2015 | DOI: 10.1002/cbic.201500081
Heparinases cleave heparin and heparan sulfate (HS) by an elimination mechanism and are important biologics for anticoagulation drug production and for heparin and HS characterisation. Defined HS oligosaccharides were exploited to study the substrate specificity of heparinase II from two different microbial organisms.
- Functional Characterization of Different ORFs Including Luciferase-Like Monooxygenase Genes from the Mensacarcin Gene Cluster
Sarah Maier, Tanja Heitzler, Dr. Katharina Asmus, Dr. Elke Brötz, Dr. Uwe Hardter, Katharina Hesselbach, Dr. Thomas Paululat and Prof. Dr. Andreas Bechthold
Article first published online: 23 APR 2015 | DOI: 10.1002/cbic.201500048
MsnO2, MsnO4, and MsnO8: We elucidated the components of the Streptomyces bottropensis mensacarcin biosynthesis gene cluster by selective deletion and complementation in a heterologous expression system. Three luciferase-like monooxygenases are involved in later steps of mensacarcin biosynthesis.