학술논문

α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles
Document Type
article
Source
International Journal of Molecular Sciences, Vol 22, Iss 11, p 5412 (2021)
Subject
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)
Biology (General)
QH301-705.5
Chemistry
QD1-999
Language
English
ISSN
22115412
1422-0067
1661-6596
Abstract
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.