Abstract Post-translationally modified proteins make up the majority of the proteome and establish, to a large part, the impressive level of functional diversity in higher, multi-cellular organisms. Most eukaryotic post-translational protein modifications (PTMs) denote reversible, covalent additions of small chemical entities such as phosphate-, acyl-, alkyl- and glycosyl-groups onto selected subsets of modifiable amino acids. In turn, these modifications induce highly specific changes in the chemical environments of individual protein residues, which are readily detected by high-resolution NMR spectroscopy. In the following, we provide a concise compendium of NMR characteristics of the main types of eukaryotic PTMs: serine, threonine, tyrosine and histidine phosphorylation, lysine acetylation, lysine and arginine methylation, and serine, threonine O-glycosylation. We further delineate the previously uncharacterized NMR properties of lysine propionylation, butyrylation, succinylation, malonylation and crotonylation, which, altogether, define an initial reference frame for comprehensive PTM studies by high-resolution NMR spectroscopy.
Content Type Journal Article
Category Perspective
Pages 1-20
DOI 10.1007/s10858-012-9674-x
Authors
Francois-Xavier Theillet, Department of NMR-Supported Structural Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin), In-cell NMR Group, Robert-Roessle Strasse 10, 13125 Berlin, Germany
Caroline Smet-Nocca, CNRS UMR 8576, Universite Lille Nord de France, 59655 Villeneuve dâ??Ascq, France
Stamatios Liokatis, Department of NMR-Supported Structural Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin), In-cell NMR Group, Robert-Roessle Strasse 10, 13125 Berlin, Germany
Rossukon Thongwichian, Department of NMR-Supported Structural Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin), In-cell NMR Group, Robert-Roessle Strasse 10, 13125 Berlin, Germany
Jonas Kosten, Department of NMR-Supported Structural Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin), In-cell NMR Group, Robert-Roessle Strasse 10, 13125 Berlin, Germany
Mi-Kyung Yoon, Department of Structural Biology, St. Jude Childrenâ??s Research Hospital, Memphis, TN, USA
Richard W. Kriwacki, Department of Structural Biology, St. Jude Childrenâ??s Research Hospital, Memphis, TN, USA
Isabelle Landrieu, CNRS UMR 8576, Universite Lille Nord de France, 59655 Villeneuve dâ??Ascq, France
Guy Lippens, CNRS UMR 8576, Universite Lille Nord de France, 59655 Villeneuve dâ??Ascq, France
Philipp Selenko, Department of NMR-Supported Structural Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin), In-cell NMR Group, Robert-Roessle Strasse 10, 13125 Berlin, Germany
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Cell signaling, post-translational protein modifications and NMR spectroscopy
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