Directed evolution of SecB chaperones toward toxin-antitoxin systems

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Directed evolution of SecB chaperones toward toxin-antitoxin systems.

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 facilitati...

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Toxin-antitoxin (TA) systems are small genetic elements composed of a toxin gene and its cognate antitoxin. The toxins of all known TA systems are proteins while the antitoxins are either proteins or non-coding RNAs. Based on the molecular nature of the antitoxin and its mode of interaction with the toxin the TA modules are currently grouped into five classes. In general, the toxin is more stab...

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Bacterial toxin-antitoxin systems

Toxin-antitoxin (TA) systems are composed of two elements: a toxic protein and an antitoxin which is either an RNA (type I and III) or a protein (type II). Type II systems are abundant in bacterial genomes in which they move via horizontal gene transfer. They are generally composed of two genes organized in an operon, encoding a toxin and a labile antitoxin. When carried by mobile genetic eleme...

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Bacterial Toxin-antitoxin Systems Translation Inhibitors Everywhere the Toxin-antitoxin System Framework the Selfish Nature of Toxin-antitoxin Systems

*Correspondence to: Laurence Van Melderen; Email: [email protected] Toxin-antitoxin (TA) systems are composed of two elements: a toxic protein and an antitoxin which is either an RNA (type I and III) or a protein (type II). Type II systems are abundant in bacterial genomes in which theymove via horizontal gene transfer. They are generally composed of two genes organized in an operon, encoding ...

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Multitasking SecB chaperones in bacteria

Protein export in bacteria is facilitated by the canonical SecB chaperone, which binds to unfolded precursor proteins, maintains them in a translocation competent state and specifically cooperates with the translocase motor SecA to ensure their proper targeting to the Sec translocon at the cytoplasmic membrane. Besides its key contribution to the Sec pathway, SecB chaperone tasking is critical ...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 2017

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.1710456114