Engineering Af1521 improves ADP-ribose binding and identification of ADP-ribosylated proteins

Kathrin Nowak; Florian Rosenthal; Tobias Karlberg; Mareike Bütepage; Ann-Gerd Thorsell; Birgit Dreier; Jonas Grossmann; Jens Sobek; Ralph Imhof; Bernhard Lüscher; Herwig Schüler; Andreas Plückthun; Deena M. Leslie Pedrioli; Michael O. Hottiger

doi:10.1038/s41467-020-18981-w

Nature Communications (Oct 2020)

Engineering Af1521 improves ADP-ribose binding and identification of ADP-ribosylated proteins

Kathrin Nowak,
Florian Rosenthal,
Tobias Karlberg,
Mareike Bütepage,
Ann-Gerd Thorsell,
Birgit Dreier,
Jonas Grossmann,
Jens Sobek,
Ralph Imhof,
Bernhard Lüscher,
Herwig Schüler,
Andreas Plückthun,
Deena M. Leslie Pedrioli,
Michael O. Hottiger

Affiliations

Kathrin Nowak: Department of Molecular Mechanisms of Disease, University of Zurich
Florian Rosenthal: Department of Molecular Mechanisms of Disease, University of Zurich
Tobias Karlberg: Department of Biosciences and Nutrition, Karolinska Institute
Mareike Bütepage: Institute of Biochemistry and Molecular Biology, RWTH Aachen University
Ann-Gerd Thorsell: Department of Biosciences and Nutrition, Karolinska Institute
Birgit Dreier: Department of Biochemistry, University of Zurich
Jonas Grossmann: Functional Genomics Center Zurich, ETH Zurich and University of Zurich
Jens Sobek: Functional Genomics Center Zurich, ETH Zurich and University of Zurich
Ralph Imhof: Department of Molecular Mechanisms of Disease, University of Zurich
Bernhard Lüscher: Institute of Biochemistry and Molecular Biology, RWTH Aachen University
Herwig Schüler: Department of Biosciences and Nutrition, Karolinska Institute
Andreas Plückthun: Department of Biochemistry, University of Zurich
Deena M. Leslie Pedrioli: Department of Molecular Mechanisms of Disease, University of Zurich
Michael O. Hottiger: Department of Molecular Mechanisms of Disease, University of Zurich

DOI: https://doi.org/10.1038/s41467-020-18981-w
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 14

Abstract

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ADP-ribose binding macro domains facilitate the enrichment and detection of cellular ADP-ribosylation. Here, the authors generate an engineered macro domain with increased ADP-ribose affinity, improving the identification of ADP-ribosylated proteins by proteomics, western blot and immunofluorescence.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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