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dc.contributor.author
Macé, Kevin
dc.contributor.author
Meir, Amit
dc.contributor.author
Lukoyanova, Natalya
dc.contributor.author
Liu, Luying
dc.contributor.author
Chetrit, David
dc.contributor.author
Hospenthal, Manuela
dc.contributor.author
Roy, Craig R.
dc.contributor.author
Waksman, Gabriel
dc.date.accessioned
2022-02-15T14:54:10Z
dc.date.available
2022-01-24T12:48:41Z
dc.date.available
2022-01-25T07:04:12Z
dc.date.available
2022-01-26T10:12:22Z
dc.date.available
2022-02-15T14:54:10Z
dc.date.issued
2022-02
dc.identifier.issn
0950-382x
dc.identifier.issn
1365-2958
dc.identifier.other
10.1111/mmi.14847
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/527886
dc.identifier.doi
10.3929/ethz-b-000527886
dc.description.abstract
Legionella pneumophila is an opportunistic pathogen infecting alveolar macrophages and protozoa species. Legionella utilizes a Type IV Secretion System (T4SS) to translocate over 300 effector proteins into its host cell. In a recent study, we have isolated and solved the cryo-EM structure of the Type IV Coupling Complex (T4CC), a large cytoplasmic determinant associated with the inner membrane that recruits effector proteins for delivery to the T4SS for translocation. The T4CC is composed of a DotLMNYZ hetero-pentameric core from which the flexible IcmSW module flexibly protrudes. The DotY and DotZ proteins were newly reported members of this complex and their role remained elusive. In this study, we observed the effect of deleting DotY and DotZ on T4CC stability and localization. Furthermore, we found these two proteins are co-dependent, whereby the deletion of DotY resulted in DotZ absence from the coupling complex, and vice versa. Additional cryo-EM data analysis revealed the dynamic movement of the IcmSW module is modified by the DotY/Z proteins. We therefore determined the likely function of DotY and DotZ and revealed their importance on T4CC function.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Wiley
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.subject
coupling complex
en_US
dc.subject
effector recruitment
en_US
dc.subject
Legionella pneumophila
en_US
dc.subject
recruitment platform
en_US
dc.subject
type 4 secretion system
en_US
dc.title
Proteins DotY and DotZ modulate the dynamics and localization of the type IVB coupling complex of Legionella pneumophila
en_US
dc.type
Journal Article
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
dc.date.published
2021-11-24
ethz.journal.title
Molecular Microbiology
ethz.journal.volume
117
en_US
ethz.journal.issue
2
en_US
ethz.journal.abbreviated
Mol Microbiol
ethz.pages.start
307
en_US
ethz.pages.end
319
en_US
ethz.size
13 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
s.l.
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02521 - Inst. f. Molekularbiologie u. Biophysik / Inst. Molecular Biology and Biophysics
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02521 - Inst. f. Molekularbiologie u. Biophysik / Inst. Molecular Biology and Biophysics::09756 - Hospenthal, Manuela / Hospenthal, Manuela
en_US
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02521 - Inst. f. Molekularbiologie u. Biophysik / Inst. Molecular Biology and Biophysics::09756 - Hospenthal, Manuela / Hospenthal, Manuela
ethz.identifier.orcidWorkCode
106889170
ethz.date.deposited
2022-01-24T12:48:47Z
ethz.source
FORM
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2022-02-15T14:54:16Z
ethz.rosetta.lastUpdated
2023-02-07T00:14:16Z
ethz.rosetta.versionExported
true
ethz.COinS
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