- SASDAU8: Immunosuppressive virulence protein YopM (Yersinia outer protein ... -
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Open data
ID or keywords:
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Basic information
Entry
Database: SASBDB / ID: SASDAU8
Sample
Immunosuppressive virulence protein YopM
Yersinia outer protein M (34-481) (protein), YopM, Yersinia enterocolitica
Biological species
Yersinia enterocolitica (bacteria)
Citation
Journal: PLoS Pathog / Year: 2016 Title: Immunosuppressive Yersinia Effector YopM Binds DEAD Box Helicase DDX3 to Control Ribosomal S6 Kinase in the Nucleus of Host Cells. Authors: Laura Berneking / Marie Schnapp / Andreas Rumm / Claudia Trasak / Klaus Ruckdeschel / Malik Alawi / Adam Grundhoff / Alexey G Kikhney / Friedrich Koch-Nolte / Friedrich Buck / Markus ...Authors: Laura Berneking / Marie Schnapp / Andreas Rumm / Claudia Trasak / Klaus Ruckdeschel / Malik Alawi / Adam Grundhoff / Alexey G Kikhney / Friedrich Koch-Nolte / Friedrich Buck / Markus Perbandt / Christian Betzel / Dmitri I Svergun / Moritz Hentschke / Martin Aepfelbacher / Abstract: Yersinia outer protein M (YopM) is a crucial immunosuppressive effector of the plaque agent Yersinia pestis and other pathogenic Yersinia species. YopM enters the nucleus of host cells but neither ...Yersinia outer protein M (YopM) is a crucial immunosuppressive effector of the plaque agent Yersinia pestis and other pathogenic Yersinia species. YopM enters the nucleus of host cells but neither the mechanisms governing its nucleocytoplasmic shuttling nor its intranuclear activities are known. Here we identify the DEAD-box helicase 3 (DDX3) as a novel interaction partner of Y. enterocolitica YopM and present the three-dimensional structure of a YopM:DDX3 complex. Knockdown of DDX3 or inhibition of the exportin chromosomal maintenance 1 (CRM1) increased the nuclear level of YopM suggesting that YopM exploits DDX3 to exit the nucleus via the CRM1 export pathway. Increased nuclear YopM levels caused enhanced phosphorylation of Ribosomal S6 Kinase 1 (RSK1) in the nucleus. In Y. enterocolitica infected primary human macrophages YopM increased the level of Interleukin-10 (IL-10) mRNA and this effect required interaction of YopM with RSK and was enhanced by blocking YopM's nuclear export. We propose that the DDX3/CRM1 mediated nucleocytoplasmic shuttling of YopM determines the extent of phosphorylation of RSK in the nucleus to control transcription of immunosuppressive cytokines.
Contact author
Al Kikhney (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)
Instrument name: PETRA III P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotron / Wavelength: 0.12 Å / Dist. spec. to detc.: 3.1 mm
Detector
Name: Pilatus 2M
Scan
Title: YopM is dimer in solution / Measurement date: Nov 13, 2013 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 0.05 sec. / Number of frames: 20 / Unit: 1/nm /
Min
Max
Q
0.0817
4.4911
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 779 /
Min
Max
Q
0.10545
2.15471
P(R) point
1
779
R
0
11.5
Result
Type of curve: extrapolated / Comments: YopM_34-481 is a dimer in solution
Experimental
Experimental error
Porod
Porod error
MW
108 kDa
11
96 kDa
10
Volume
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-
153.8 nm3
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Guinier
P(R)
Guinier error
Forward scattering, I0
16939.3
-
-
Radius of gyration, Rg
3.88 nm
3.855 nm
0.11
Min
Max
Error
D
-
11.5
1.2
Guinier point
1
85
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