Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 118, Issue 7, Pages -Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.2008500118
Keywords
type VI secretion system; TssA; TagB; sheath stabilization; Pseudomonas
Categories
Funding
- Medical Research Council (MRC) [MR/N023250/1, MRK/K001930]
- Biotechnology and Biological Sciences Research Council (BBSRC) [BB/N02539/1]
- MRC Career Development Award [MR/M009505/1]
- MRC
- European Commission Marie Curie Fellowship H2020-MSCA-IF-2014 [654135]
- InterTalentum Fellowship - (European Commission) [GA713366]
- InterTalentum Fellowship - (Universidad Autonoma de Madrid) [GA713366]
- Research Challenges 2018 R+D+i Project - (Spanish Ministry of Science, Innovation, and Universities) [RTI2018-096936-J-I00]
- Wellcome Trust [104931/Z/14/Z]
- BBSRC [BB/L015129/1]
- BBSRC [BB/L015129/1, BB/N002539/1, BB/M02735X/1] Funding Source: UKRI
- MRC [MR/S02316X/1, 2367527, MR/N023250/1, MR/M009505/1, MR/P028225/1, MR/K001930/1] Funding Source: UKRI
- Marie Curie Actions (MSCA) [654135] Funding Source: Marie Curie Actions (MSCA)
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The T6SS is a nanomachine primarily involved in interbacterial competition, with TssA being a key component for its assembly. Researchers have found unexpected diversity in TssA proteins, with a short form and a long form existing. The discovery of structural components that interact with short TssA proteins sheds light on the mechanisms for T6SS assembly and functioning.
The type VI secretion system (T6SS) is a phage-derived contractile nanomachine primarily involved in interbacterial competition. Its pivotal component, TssA, is indispensable for the assembly of the T6SS sheath structure, the contraction of which propels a payload of effector proteins into neighboring cells. Despite their key function, TssA proteins exhibit unexpected diversity and exist in two major forms, a short form (TssA(S)) and a long form (TssA(L)). While TssA(L) proteins interact with a partner, called TagA, to anchor the distal end of the extended sheath, the mechanism for the stabilization of TssA(S)-containing T6SSs remains unknown. Here we discover a class of structural components that interact with short TssA proteins and contribute to T6SS assembly by stabilizing the polymerizing sheath from the baseplate. We demonstrate that the presence of these components is important for full sheath extension and optimal firing. Moreover, we show that the pairing of each form of TssA with a different class of sheath stabilization proteins results in T6SS apparatuses that either reside in the cell for some time or fire immediately after sheath extension. We propose that this diversity in firing dynamics could contribute to the specialization of the T6SS to suit bacterial lifestyles in diverse environmental niches.
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