Structure-function analysis of VapB4 antitoxin identifies critical features of a minimal VapC4 toxin-binding module.

ABSTRACT:

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Bacterial toxin-antitoxin systems play a critical role in the regulation of gene expression, leading to developmental changes, reversible dormancy, and cell death. Type II toxin-antitoxin pairs, composed of protein toxins and antitoxins, exist in nearly all bacteria and are classified into six groups on the basis of the structure of the toxins. The VapBC group comprises the most common type II system and, like other toxin-antitoxin systems, functions to elicit dormancy by inhibiting protein synthesis. Activation of toxin function requires protease degradation of the VapB antitoxin, which frees the VapC toxin from the VapBC complex, allowing it to hydrolyze the RNAs required for translation. Generally, type II antitoxins bind with high specificity to their cognate toxins

SUBMITTER: Jin G 

PROVIDER: S-EPMC4352670 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature