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  Site-Specific Detection of Arginine Methylation in Highly Repetitive Protein Motifs of Low Sequence Complexity by NMR

Altincekic, N., Löhr, F., Meier-Credo, J., Langer, J. D., Hengesbach, M., Richter, C., et al. (2020). Site-Specific Detection of Arginine Methylation in Highly Repetitive Protein Motifs of Low Sequence Complexity by NMR. Journal of the American Chemical Society, 142(16), 7647-7654. doi:10.1021/jacs.0c02308.

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 Creators:
Altincekic, Nadide1, 2, Author
Löhr, Frank2, 3, Author
Meier-Credo, Jakob4, Author                 
Langer, Julian David4, Author                 
Hengesbach, Martin1, Author
Richter, Christian1, 2, Author
Schwalbe, Harald1, 2, Author
Affiliations:
1Institute for Organic Chemistry and Chemical Biology, Goethe University Frankfurt am Main, Frankfurt 60438, Germany, ou_persistent22              
2Center of Biomolecular Magnetic Resonance (BMRZ), Goethe University Frankfurt am Main, Frankfurt 60438, Germany, ou_persistent22              
3Institute of Biophysical Chemistry, Goethe University Frankfurt am Main, Frankfurt 60438, Germany, ou_persistent22              
4Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society, ou_3262216              

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Free keywords: Guanidine; Peptides and proteins; Monomers; Organic reactions; Nitrogen
 Abstract: Post-translational modifications of proteins are widespread in eukaryotes. To elucidate the functional role of these modifications, detection methods need to be developed that provide information at atomic resolution. Here, we report on the development of a novel Arg-specific NMR experiment that detects the methylation status and symmetry of each arginine side chain even in highly repetitive RGG amino acid sequence motifs found in numerous proteins within intrinsically disordered regions. The experiment relies on the excellent resolution of the backbone H,N correlation spectra even in these low complexity sequences. It requires 13C, 15N labeled samples.

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Language(s): eng - English
 Dates: 2020-02-272020-04-012020-04-012020-04-22
 Publication Status: Issued
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/jacs.0c02308
 Degree: -

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Title: Journal of the American Chemical Society
  Other : JACS
  Abbreviation : J. Am. Chem. Soc.
Source Genre: Journal
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Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 142 (16) Sequence Number: - Start / End Page: 7647 - 7654 Identifier: ISSN: 0002-7863
CoNE: https://pure.mpg.de/cone/journals/resource/954925376870