Journal
CELL REPORTS
Volume 32, Issue 12, Pages -Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2020.108161
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Funding
- National Natural Science Foundation of China [31500050, 31800054, 31270786]
- academic promotion programme of Shandong First Medical University [2019LJ001]
- Innovation Project of Shandong Academy of Medical Sciences
- Primary Research and Development Plan of Shandong Province [2019GSF107026, 2019GSF107055]
- Natural Science Foundation of Shandong Province [ZR2017MH020]
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Sensing stressful conditions and adjusting the cellular metabolism to adapt to the environment are essential activities for bacteria to survive in variable situations. Here, we describe a stress-related protein, YdiU, and characterize YdiU as an enzyme that catalyzes the covalent attachment of uridine-5 '-monophosphate to a protein tyrosine/histidine residue, an unusual modification defined as UMPylation. Mn2+ serves as an essential co-factor for YdiU-mediated UMPylation. UTP and Mn2+ binding converts YdiU to an aggregate-prone state facilitating the recruitment of chaperones. The UMPylation of chaperones prevents them from binding co-factors or clients, thereby impairing their function. Consistent with the recent finding that YdiU acts as an AMPylator, we further demonstrate that the self-AMPylation of YdiU padlocks its chaperone-UMPylation activity. A detailed mechanism is proposed based on the crystal structures of Apo-YdiU and YdiU-AMPNPP-Mn2+ and on molecular dynamics simulation models of YdiU-UTP-Mn2+ and YdiU-UTP-peptide. In vivo data demonstrate that YdiU effectively protects Salmonella from stress-induced ATP depletion through UMPylation.
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