期刊
MOLECULAR MICROBIOLOGY
卷 117, 期 2, 页码 307-319出版社
WILEY
DOI: 10.1111/mmi.14847
关键词
coupling complex; effector recruitment; Legionella pneumophila; recruitment platform; type 4 secretion system
资金
- ERC [321630]
- Wellcome [217089, 202679/Z/16/Z, 206166/Z/17/Z]
- NIAID [R21AI130671, R37AI041699]
- Medical Research Council UK
- Biotechnology and Biological Sciences Research Council
- Wellcome Trust [202679/Z/16/Z, 206166/Z/17/Z] Funding Source: Wellcome Trust
- European Research Council (ERC) [321630] Funding Source: European Research Council (ERC)
The study revealed the significance of DotY and DotZ in maintaining the stability and localization of T4CC, with these two proteins showing a codependent relationship. Additionally, DotY and DotZ were found to regulate the dynamic movement of the IcmSW module.
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.
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