α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles
Type III Secretion Systems (T3SSs) are multicomponent nanomachines located at the cell envelope of Gram-negative bacteria. Their main function is to transport bacterial proteins either extracellularly or directly into the eukaryotic host cell cytoplasm. Type III Secretion effectors (T3SEs), latest t...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-05-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/22/11/5412 |
| _version_ | 1797533301949333504 |
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| author | Anastasia D. Gazi Michael Kokkinidis Vasiliki E. Fadouloglou |
| author_facet | Anastasia D. Gazi Michael Kokkinidis Vasiliki E. Fadouloglou |
| author_sort | Anastasia D. Gazi |
| collection | DOAJ |
| description | Type III Secretion Systems (T3SSs) are multicomponent nanomachines located at the cell envelope of Gram-negative bacteria. Their main function is to transport bacterial proteins either extracellularly or directly into the eukaryotic host cell cytoplasm. Type III Secretion effectors (T3SEs), latest to be secreted T3S substrates, are destined to act at the eukaryotic host cell cytoplasm and occasionally at the nucleus, hijacking cellular processes through mimicking eukaryotic proteins. A broad range of functions is attributed to T3SEs, ranging from the manipulation of the host cell’s metabolism for the benefit of the bacterium to bypassing the host’s defense mechanisms. To perform this broad range of manipulations, T3SEs have evolved numerous novel folds that are compatible with some basic requirements: they should be able to easily unfold, pass through the narrow T3SS channel, and refold to an active form when on the other side. In this review, the various folds of T3SEs are presented with the emphasis placed on the functional and structural importance of α-helices and helical domains. |
| first_indexed | 2024-03-10T11:12:36Z |
| format | Article |
| id | doaj.art-ccbf7afc5ecf4ae5a4d6b0f8c97f661a |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T11:12:36Z |
| publishDate | 2021-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-ccbf7afc5ecf4ae5a4d6b0f8c97f661a2023-11-21T20:40:55ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-05-012211541210.3390/ijms22115412α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile RolesAnastasia D. Gazi0Michael Kokkinidis1Vasiliki E. Fadouloglou2Unit of Technology & Service Ultrastructural Bio-Imaging (UTechS UBI), Institut Pasteur, 75015 Paris, FranceInstitute of Molecular Biology and Biotechnology, Foundation for Research and Technology-Hellas, Nikolaou Plastira 100, Heraklion, 70013 Crete, GreeceDepartment of Molecular Biology & Genetics, Democritus University of Thrace, 68100 Alexandroupolis, GreeceType III Secretion Systems (T3SSs) are multicomponent nanomachines located at the cell envelope of Gram-negative bacteria. Their main function is to transport bacterial proteins either extracellularly or directly into the eukaryotic host cell cytoplasm. Type III Secretion effectors (T3SEs), latest to be secreted T3S substrates, are destined to act at the eukaryotic host cell cytoplasm and occasionally at the nucleus, hijacking cellular processes through mimicking eukaryotic proteins. A broad range of functions is attributed to T3SEs, ranging from the manipulation of the host cell’s metabolism for the benefit of the bacterium to bypassing the host’s defense mechanisms. To perform this broad range of manipulations, T3SEs have evolved numerous novel folds that are compatible with some basic requirements: they should be able to easily unfold, pass through the narrow T3SS channel, and refold to an active form when on the other side. In this review, the various folds of T3SEs are presented with the emphasis placed on the functional and structural importance of α-helices and helical domains.https://www.mdpi.com/1422-0067/22/11/5412Type III Secretion System (T3SS)Type III Secretion effector (T3SE)dictionary of secondary structure in proteins (DSSP)4-α-helix bundlecoiled coilNovel E3 Ligase (NEL) |
| spellingShingle | Anastasia D. Gazi Michael Kokkinidis Vasiliki E. Fadouloglou α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles International Journal of Molecular Sciences Type III Secretion System (T3SS) Type III Secretion effector (T3SE) dictionary of secondary structure in proteins (DSSP) 4-α-helix bundle coiled coil Novel E3 Ligase (NEL) |
| title | α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles |
| title_full | α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles |
| title_fullStr | α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles |
| title_full_unstemmed | α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles |
| title_short | α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles |
| title_sort | α helices in the type iii secretion effectors a prevalent feature with versatile roles |
| topic | Type III Secretion System (T3SS) Type III Secretion effector (T3SE) dictionary of secondary structure in proteins (DSSP) 4-α-helix bundle coiled coil Novel E3 Ligase (NEL) |
| url | https://www.mdpi.com/1422-0067/22/11/5412 |
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