Chemical proteomic profiling reveals protein interactors of the alarmones diadenosine triphosphate and tetraphosphate

Lena Krüger, Christoph J. Albrecht, Hannah K. Schammann, Florian M. Stumpf, Marie L. Niedermeier, Yizhi Yuan, Katrin Stuber, Josua Wimmer, Florian Stengel, Martin Scheffner and Andreas Marx ()
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Lena Krüger: University of Konstanz
Christoph J. Albrecht: University of Konstanz
Hannah K. Schammann: University of Konstanz
Florian M. Stumpf: University of Konstanz
Marie L. Niedermeier: University of Konstanz
Yizhi Yuan: University of Konstanz
Katrin Stuber: University of Konstanz
Josua Wimmer: University of Konstanz
Florian Stengel: University of Konstanz
Martin Scheffner: University of Konstanz
Andreas Marx: University of Konstanz

Nature Communications, 2021, vol. 12, issue 1, 1-13

Abstract: Abstract The nucleotides diadenosine triphosphate (Ap3A) and diadenosine tetraphosphate (Ap4A) are formed in prokaryotic and eukaryotic cells. Since their concentrations increase significantly upon cellular stress, they are considered to be alarmones triggering stress adaptive processes. However, their cellular roles remain elusive. To elucidate the proteome-wide interactome of Ap3A and Ap4A and thereby gain insights into their cellular roles, we herein report the development of photoaffinity-labeling probes and their employment in chemical proteomics. We demonstrate that the identified ApnA interactors are involved in many fundamental cellular processes including carboxylic acid and nucleotide metabolism, gene expression, various regulatory processes and cellular response mechanisms and only around half of them are known nucleotide interactors. Our results highlight common functions of these ApnAs across the domains of life, but also identify those that are different for Ap3A or Ap4A. This study provides a rich source for further functional studies of these nucleotides and depicts useful tools for characterization of their regulatory mechanisms in cells.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-26075-4

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DOI: 10.1038/s41467-021-26075-4

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