Ubiquitination independent of E1 and E2 enzymes by bacterial effectors

doi:10.1038/nature17657

CORC > 北京大学 > 化学与分子工程学院

	Ubiquitination independent of E1 and E2 enzymes by bacterial effectors
	Qiu, Jiazhang ; Sheedlo, Michael J. ; Yu, Kaiwen ; Tan, Yunhao ; Nakayasu, Ernesto S. ; Das, Chittaranjan ; Liu, Xiaoyun ; Luo, Zhao-Qing
刊名	NATURE
	2016
关键词	LEGIONELLA-PNEUMOPHILA ENDOPLASMIC-RETICULUM SUBSTRATE RECOGNITION STRUCTURAL BASIS CELL BIOLOGY PROTEIN SYSTEM FAMILY PHAGOSOME REPLICATION
DOI	10.1038/nature17657
英文摘要	Signalling by ubiquitination regulates virtually every cellular process in eukaryotes. Covalent attachment of ubiquitin to a substrate is catalysed by the E1, E2 and E3 three-enzyme cascade(1), which links the carboxy terminus of ubiquitin to the e-amino group of, in most cases, a lysine of the substrate via an isopeptide bond. Given the essential roles of ubiquitination in the regulation of the immune system, it is not surprising that the ubiquitination network is a common target for diverse infectious agents(2). For example, many bacterial pathogens exploit ubiquitin signalling using virulence factors that function as E3 ligases, deubiquitinases3 or as enzymes that directly attack ubiquitin(4). The bacterial pathogen Legionella pneumophila utilizes approximately 300 effectors that modulate diverse host processes to create a permissive niche for its replication in phagocytes(5). Here we demonstrate that members of the SidE effector family of L. pneumophila ubiquitinate multiple Rab small GTPases associated with the endoplasmic reticulum. Moreover, we show that these proteins are capable of catalysing ubiquitination without the need for the E1 and E2 enzymes. A putative mono-ADP-ribosyltransferase motif critical for the ubiquitination activity is also essential for the role of the SidE family in intracellular bacterial replication in a protozoan host. The E1/E2-independent ubiquitination catalysed by these enzymes is energized by nicotinamide adenine dinucleotide, which activates ubiquitin by the formation of ADP-ribosylated ubiquitin. These results establish that ubiquitination can be catalysed by a single enzyme, the activity of which does not require ATP.; National Institutes of Health [R56AI103168, K02AI085403, R21AI105714, 2R01GM103401]; National Natural Science Foundation of China [21305006, 21475005]; SCI(E); PubMed; ARTICLE; luoz@purdue.edu; 7601; 120-+; 533
语种	中文
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/434228]
专题	化学与分子工程学院
推荐引用方式 GB/T 7714	Qiu, Jiazhang,Sheedlo, Michael J.,Yu, Kaiwen,et al. Ubiquitination independent of E1 and E2 enzymes by bacterial effectors[J]. NATURE,2016.
APA	Qiu, Jiazhang.,Sheedlo, Michael J..,Yu, Kaiwen.,Tan, Yunhao.,Nakayasu, Ernesto S..,...&Luo, Zhao-Qing.(2016).Ubiquitination independent of E1 and E2 enzymes by bacterial effectors.NATURE.
MLA	Qiu, Jiazhang,et al."Ubiquitination independent of E1 and E2 enzymes by bacterial effectors".NATURE (2016).