A novel stabilization mechanism for the type VI secretion system sheath

Author:

Bernal PatriciaORCID,Furniss R. Christopher D.ORCID,Fecht Selina,Leung Rhoda C. Y.ORCID,Spiga Livia,Mavridou Despoina A. I.,Filloux AlainORCID

Abstract

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 (TssAS) and a long form (TssAL). While TssAL proteins interact with a partner, called TagA, to anchor the distal end of the extended sheath, the mechanism for the stabilization of TssAS-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.

Funder

RCUK | Medical Research Council

RCUK | Biotechnology and Biological Sciences Research Council

European Commission

Spanish Ministry of Science, Innovation and Universities

Wellcome

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

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