Research ExplorerPublicationsPronucleotide Probes Reveal a Diverging Specificity for AMPy...

Pronucleotide Probes Reveal a Diverging Specificity for AMPylation vs UMPylation of Human and Bacterial Nucleotide Transferases

Standard

Pronucleotide Probes Reveal a Diverging Specificity for AMPylation vs UMPylation of Human and Bacterial Nucleotide Transferases. / Mostert, Dietrich; Bubeneck, Wilhelm Andrei; Rauh, Theresa; Kielkowski, Pavel; Itzen, Aymelt; Jung, Kirsten; Sieber, Stephan A.

In: BIOCHEMISTRY-US, Vol. 63, No. 5, 05.03.2024, p. 651-659.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Mostert, D, Bubeneck, WA, Rauh, T, Kielkowski, P, Itzen, A, Jung, K & Sieber, SA 2024, 'Pronucleotide Probes Reveal a Diverging Specificity for AMPylation vs UMPylation of Human and Bacterial Nucleotide Transferases', BIOCHEMISTRY-US, vol. 63, no. 5, pp. 651-659. https://doi.org/10.1021/acs.biochem.3c00568

APA

Mostert, D., Bubeneck, W. A., Rauh, T., Kielkowski, P., Itzen, A., Jung, K., & Sieber, S. A. (2024). Pronucleotide Probes Reveal a Diverging Specificity for AMPylation vs UMPylation of Human and Bacterial Nucleotide Transferases. BIOCHEMISTRY-US, 63(5), 651-659. https://doi.org/10.1021/acs.biochem.3c00568

Vancouver

Mostert D, Bubeneck WA, Rauh T, Kielkowski P, Itzen A, Jung K et al. Pronucleotide Probes Reveal a Diverging Specificity for AMPylation vs UMPylation of Human and Bacterial Nucleotide Transferases. BIOCHEMISTRY-US. 2024 Mar 5;63(5):651-659. https://doi.org/10.1021/acs.biochem.3c00568

Bibtex

@article{6097a0df956544e3a15ddeec04bf353e,
title = "Pronucleotide Probes Reveal a Diverging Specificity for AMPylation vs UMPylation of Human and Bacterial Nucleotide Transferases",
abstract = "AMPylation is a post-translational modification utilized by human and bacterial cells to modulate the activity and function of specific proteins. Major AMPylators such as human FICD and bacterial VopS have been studied extensively for their substrate and target scope in vitro. Recently, an AMP pronucleotide probe also facilitated the in situ analysis of AMPylation in living cells. Based on this technology, we here introduce a novel UMP pronucleotide probe and utilize it to profile uninfected and Vibrio parahaemolyticus infected human cells. Mass spectrometric analysis of labeled protein targets reveals an unexpected promiscuity of human nucleotide transferases with an almost identical target set of AMP- and UMPylated proteins. Vice versa, studies in cells infected by V. parahaemolyticus and its effector VopS revealed solely AMPylation of host enzymes, highlighting a so far unknown specificity of this transferase for ATP. Taken together, pronucleotide probes provide an unprecedented insight into the in situ activity profile of crucial nucleotide transferases, which can largely differ from their in vitro activity.",
keywords = "Humans, Nucleotides/metabolism, Transferases/metabolism, Bacterial Proteins/chemistry, Adenosine Monophosphate/metabolism, Protein Processing, Post-Translational",
author = "Dietrich Mostert and Bubeneck, {Wilhelm Andrei} and Theresa Rauh and Pavel Kielkowski and Aymelt Itzen and Kirsten Jung and Sieber, {Stephan A}",
year = "2024",
month = mar,
day = "5",
doi = "10.1021/acs.biochem.3c00568",
language = "English",
volume = "63",
pages = "651--659",
journal = "BIOCHEMISTRY-US",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "5",

}

RIS

TY - JOUR

T1 - Pronucleotide Probes Reveal a Diverging Specificity for AMPylation vs UMPylation of Human and Bacterial Nucleotide Transferases

AU - Mostert, Dietrich

AU - Bubeneck, Wilhelm Andrei

AU - Rauh, Theresa

AU - Kielkowski, Pavel

AU - Itzen, Aymelt

AU - Jung, Kirsten

AU - Sieber, Stephan A

PY - 2024/3/5

Y1 - 2024/3/5

N2 - AMPylation is a post-translational modification utilized by human and bacterial cells to modulate the activity and function of specific proteins. Major AMPylators such as human FICD and bacterial VopS have been studied extensively for their substrate and target scope in vitro. Recently, an AMP pronucleotide probe also facilitated the in situ analysis of AMPylation in living cells. Based on this technology, we here introduce a novel UMP pronucleotide probe and utilize it to profile uninfected and Vibrio parahaemolyticus infected human cells. Mass spectrometric analysis of labeled protein targets reveals an unexpected promiscuity of human nucleotide transferases with an almost identical target set of AMP- and UMPylated proteins. Vice versa, studies in cells infected by V. parahaemolyticus and its effector VopS revealed solely AMPylation of host enzymes, highlighting a so far unknown specificity of this transferase for ATP. Taken together, pronucleotide probes provide an unprecedented insight into the in situ activity profile of crucial nucleotide transferases, which can largely differ from their in vitro activity.

AB - AMPylation is a post-translational modification utilized by human and bacterial cells to modulate the activity and function of specific proteins. Major AMPylators such as human FICD and bacterial VopS have been studied extensively for their substrate and target scope in vitro. Recently, an AMP pronucleotide probe also facilitated the in situ analysis of AMPylation in living cells. Based on this technology, we here introduce a novel UMP pronucleotide probe and utilize it to profile uninfected and Vibrio parahaemolyticus infected human cells. Mass spectrometric analysis of labeled protein targets reveals an unexpected promiscuity of human nucleotide transferases with an almost identical target set of AMP- and UMPylated proteins. Vice versa, studies in cells infected by V. parahaemolyticus and its effector VopS revealed solely AMPylation of host enzymes, highlighting a so far unknown specificity of this transferase for ATP. Taken together, pronucleotide probes provide an unprecedented insight into the in situ activity profile of crucial nucleotide transferases, which can largely differ from their in vitro activity.

KW - Humans

KW - Nucleotides/metabolism

KW - Transferases/metabolism

KW - Bacterial Proteins/chemistry

KW - Adenosine Monophosphate/metabolism

KW - Protein Processing, Post-Translational

U2 - 10.1021/acs.biochem.3c00568

DO - 10.1021/acs.biochem.3c00568

M3 - SCORING: Journal article

C2 - 38388156

VL - 63

SP - 651

EP - 659

JO - BIOCHEMISTRY-US

JF - BIOCHEMISTRY-US

SN - 0006-2960

IS - 5

ER -