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ACS Chem Biol. 2018 Aug 17;13(8):1958-1963. doi: 10.1021/acschembio.8b00357. Epub 2018 Jul 8.

Screening a Protein Array with Synthetic Biotinylated Inorganic Polyphosphate To Define the Human PolyP-ome.

Author information

1
Medical Research Council Laboratory for Molecular Cell Biology , University College London , London , WC1E 6BT , United Kingdom.
2
Institute of Organic Chemistry , University of Freiburg , Albertstrasse 21 , 79104 Freiburg , Germany.
3
Department of Chemistry , University of Zurich , Winterthurerstrasse 190 , 8057 Zurich , Switzerland.
4
Research Unit, "Puerta del Mar" University Hospital, School of Medicine, and Institute of Biomedical Research Cadiz (INiBICA) , University of Cadiz , Cadiz , Spain.

Abstract

Phenotypes are established by tight regulation on protein functions. This regulation can be mediated allosterically, through protein binding, and covalently, through post-translational modification (PTM). The integration of an ever-increasing number of PTMs into regulatory networks enables and defines the proteome complexity. Protein PTMs can occur enzymatically and nonenzymatically. Polyphosphorylation, which is a recently discovered PTM that belongs to the latter category, is the covalent attachment of the linear ortho-phosphate polymer called inorganic polyphosphate (polyP) to lysine residues. PolyP, which is ubiquitously present in nature, is also known to allosterically control protein function. To date, lack of reagents has prevented the systematic analysis of proteins covalently and/or allosterically associated with polyP. Here, we report on the chemical synthesis of biotin-modified monodisperse short-chain polyP (bio-polyP8-bio) and its subsequent use to screen a human proteome array to identify proteins that associate with polyP, thereby starting to define the human polyP-ome.

PMID:
29924597
DOI:
10.1021/acschembio.8b00357
[Indexed for MEDLINE]

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