| Autor: |
Jiaqi Fu, Siying Li, Hongxin Guan, Chuang Li, Yan-Bo Zhao, Tao-Tao Chen, Wei Xian, Zhengrui Zhang, Yao Liu, Qingtian Guan, Jingting Wang, Qiuhua Lu, Lina Kang, Si-Ru Zheng, Jinyu Li, Shoujing Cao, Chittaranjan Das, Xiaoyun Liu, Lei Song, Songying Ouyang, Zhao-Qing Luo |
| Jazyk: |
angličtina |
| Rok vydání: |
2024 |
| Předmět: |
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| Zdroj: |
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024) |
| Druh dokumentu: |
article |
| ISSN: |
2041-1723 |
| DOI: |
10.1038/s41467-024-50311-2 |
| Popis: |
Abstract The intracellular bacterial pathogen Legionella pneumophila modulates host cell functions by secreting multiple effectors with diverse biochemical activities. In particular, effectors of the SidE family interfere with host protein ubiquitination in a process that involves production of phosphoribosyl ubiquitin (PR-Ub). Here, we show that effector LnaB converts PR-Ub into ADP-ribosylated ubiquitin, which is further processed to ADP-ribose and functional ubiquitin by the (ADP-ribosyl)hydrolase MavL, thus maintaining ubiquitin homeostasis in infected cells. Upon being activated by actin, LnaB also undergoes self-AMPylation on tyrosine residues. The activity of LnaB requires a motif consisting of Ser, His and Glu (SHxxxE) present in a large family of toxins from diverse bacterial pathogens. Thus, our study sheds light on the mechanisms by which a pathogen maintains ubiquitin homeostasis and identifies a family of enzymes capable of protein AMPylation. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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