Ontology highlight
ABSTRACT:
SUBMITTER: Sala AJ
PROVIDER: S-EPMC5703295 | biostudies-literature | 2017 Nov
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20171107 47
SecB chaperones assist protein export in bacteria. However, certain SecB family members have diverged to become specialized toward the control of toxin-antitoxin (TA) systems known to promote bacterial adaptation to stress and persistence. In such tripartite TA-chaperone (TAC) systems, the chaperone was shown to assist folding and to prevent degradation of its cognate antitoxin, thus facilitating inhibition of the toxin. Here, we used both the export chaperone SecB of <i>Escherichia coli</i> and ...[more]