The Legionella Effector Protein DrrA AMPylates the Membrane Traffic Regulator Rab1b

被引：280

作者：

Mueller, Matthias P. ^{[1
]}

Peters, Heide ^{[1
]}

Bluemer, Julia ^{[1
]}

Blankenfeldt, Wulf ^{[1
]}

Goody, Roger S. ^{[1
]}

Itzen, Aymelt ^{[1
]}

机构：

[1] Max Planck Inst Mol Physiol, Dept Phys Biochem, D-44227 Dortmund, NRW, Germany

来源：

SCIENCE | 2010年 / 329卷 / 5994期

关键词：

GLUTAMINE-SYNTHETASE; STRUCTURAL BASIS; GTP HYDROLYSIS; ACTIVATION; GTPASES;

D O I：

10.1126/science.1192276

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

In the course of Legionnaires' disease, the bacterium Legionella pneumophila affects the intracellular vesicular trafficking of infected eukaryotic cells by recruiting the small guanosine triphosphatase (GTPase) Rab1 to the cytosolic face of the Legionella-containing vacuole. In order to accomplish this, the Legionella protein DrrA contains a specific guanine nucleotide exchange activity for Rab1 activation that exchanges guanosine triphosphate (GTP) for guanosine diphosphate on Rab1. We found that the amino-terminal domain of DrrA possesses adenosine monophosphorylation (AMPylation) activity toward the switch II region of Rab1b, leading to posttranslational covalent modification of tyrosine 77. AMPylation of switch II by DrrA restricts the access of GTPase activating proteins, thereby rendering Rab1b constitutively active.

引用

页码：946 / 949

页数：4

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