Lysine11-Linked Polyubiquitination of the AnkB F-Box Effector of Legionella pneumophila.
Infect Immun
; 84(1): 99-107, 2016 01.
Article
en En
| MEDLINE
| ID: mdl-26483404
ABSTRACT
The fate of the polyubiquitinated protein is determined by the lysine linkages involved in the polymerization of the ubiquitin monomers, which has seven lysine residues (K(6), K(11), K(27), K(29), K(33), K(48), and K(63)). The translocated AnkB effector of the intravacuolar pathogen Legionella pneumophila is a bona fide F-box protein, which is localized to the cytosolic side of the Legionella-containing vacuole (LCV) and is essential for intravacuolar proliferation within macrophages and amoebae. The F-box domain of AnkB interacts with the host SCF1 E3 ubiquitin ligase that triggers the decoration of the LCV with K(48)-linked polyubiquitinated proteins that are targeted for proteasomal degradation. Here we report that AnkB becomes rapidly polyubiquitinated within the host cell, and this modification is independent of the F-box domain of AnkB, indicating host-mediated polyubiquitination. We show that the AnkB effector interacts specifically with the host E3 ubiquitin ligase Trim21. Mass spectrometry analyses have shown that AnkB is modified by K(11)-linked polyubiquitination, which has no effect on its stability. This work shows the first example of K(11)-linked polyubiquitination of a bacterial effector and its interaction with the host Trim21 ubiquitin ligase.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Legionella pneumophila
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Ancirinas
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Proteínas Ligasas SKP Cullina F-box
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Proteínas F-Box
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Lisina
Límite:
Humans
Idioma:
En
Revista:
Infect Immun
Año:
2016
Tipo del documento:
Article
País de afiliación:
Estados Unidos