A glycine zipper motif is required for the translocation of a T6SS toxic effector into target cells.

ABSTRACT: Type VI secretion systems (T6SSs) can deliver diverse toxic effectors into eukaryotic and bacterial cells. Although much is known about the regulation and assembly of T6SS, the translocation mechanism of effectors into the periplasm and/or cytoplasm of target cells remains elusive. Here, we use the Agrobacterium tumefaciens DNase effector Tde1 to unravel the mechanism of translocation from attacker to prey. We demonstrate that Tde1 binds to its adaptor Tap1 through the N-terminus, which harbors continuous copies of GxxxG motifs resembling the glycine zipper structure found in proteins involved in the membrane channel formation. Amino acid substitutions on G³⁹ xxxG⁴³ motif do not affect Tde1-Tap1 interaction and secretion but abolish its membrane permeability and trans

SUBMITTER: Ali J 

PROVIDER: S-EPMC10240207 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature