TY - JOUR TI - Interplay between bacterial deubiquitinase and ubiquitin E3 ligase regulates ubiquitin dynamics on Legionella phagosomes AU - Liu, Shuxin AU - Luo, Jiwei AU - Zhen, Xiangkai AU - Qiu, Jiazhang AU - Ouyang, Songying AU - Luo, Zhao-Qing A2 - Harper, Wade A2 - Wolberger, Cynthia A2 - Mao, Yuxin A2 - Hartland, Elizabeth VL - 9 PY - 2020 DA - 2020/11/02 SP - e58114 C1 - eLife 2020;9:e58114 DO - 10.7554/eLife.58114 UR - https://doi.org/10.7554/eLife.58114 AB - Legionella pneumophila extensively modulates the host ubiquitin network to create the Legionella-containing vacuole (LCV) for its replication. Many of its virulence factors function as ubiquitin ligases or deubiquitinases (DUBs). Here, we identify Lem27 as a DUB that displays a preference for diubiquitin formed by K6, K11, or K48. Lem27 is associated with the LCV where it regulates Rab10 ubiquitination in concert with SidC and SdcA, two bacterial E3 ubiquitin ligases. Structural analysis of the complex formed by an active fragment of Lem27 and the substrate-based suicide inhibitor ubiquitin-propargylamide (PA) reveals that it harbors a fold resembling those in the OTU1 DUB subfamily with a Cys-His catalytic dyad and that it recognizes ubiquitin via extensive hydrogen bonding at six contact sites. Our results establish Lem27 as a DUB that functions to regulate protein ubiquitination on L. pneumophila phagosomes by counteracting the activity of bacterial ubiquitin E3 ligases. KW - Legionella pneumophila KW - type iv secretion KW - bacterial virulence KW - otu deubiquitinase JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER - 管家婆期期准免费资料精选