The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b
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The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. / Peters, Heide; Blümer, Julia; Blankenfeldt, Wulf; Goody, Roger S; Itzen, Aymelt.
In: SCIENCE, Vol. 329, No. 5994, 20.08.2010, p. 946-9.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b
AU - Peters, Heide
AU - Blümer, Julia
AU - Blankenfeldt, Wulf
AU - Goody, Roger S
AU - Itzen, Aymelt
PY - 2010/8/20
Y1 - 2010/8/20
N2 - 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.
AB - 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.
KW - Adenosine Monophosphate
KW - Animals
KW - Bacterial Proteins
KW - COS Cells
KW - Cercopithecus aethiops
KW - Crystallography
KW - Guanine Nucleotide Exchange Factors
KW - Legionella pneumophila
KW - Mass Spectrometry
KW - Models, Molecular
KW - Protein Structure, Tertiary
KW - rab GTP-Binding Proteins
KW - rab1 GTP-Binding Proteins
KW - Journal Article
KW - Research Support, Non-U.S. Gov't
U2 - 10.1126/science.1192276
DO - 10.1126/science.1192276
M3 - SCORING: Journal article
C2 - 20651120
VL - 329
SP - 946
EP - 949
JO - SCIENCE
JF - SCIENCE
SN - 0036-8075
IS - 5994
ER -