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 the 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 harbours continuous copies of GxxxG motifs, resembling the glycine zipper structure found in proteins involved in membrane channel formation. Amino acid substitutions in the G39xxxG43 motif do not affect Tde1-Tap1 interaction and Tde1 secretion but abolish its membrane permeability and the translocation

SUBMITTER: Mr. Jemal Ali 

PROVIDER: S-SCDT-10_15252-EMBR_202356849 | biostudies-other |

REPOSITORIES: biostudies-other