Article
A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase.
Proceedings of the National Academy of Sciences of the United States of America - 7 Mar 2017
Huang Qi, Alcock Felicity, Kneuper Holger, Deme Justin C, Rollauer Sarah E, Lea Susan M, Berks Ben C, Palmer Tracy
Abstract excerpt
The twin-arginine protein translocation (Tat) system mediates transport of folded proteins across the cytoplasmic membrane of bacteria and the thylakoid membrane of chloroplasts. The Tat system of Escherichia coli is made up of TatA, TatB, and TatC components. TatBC comprise the substrate receptor complex, and active Tat translocases are formed by the substrate-induced association of TatA oligomers with this...
Topics
- Amino Acid Sequence
- Amino Acid Substitution
- Arginine
- Binding Sites
- Escherichia coli
- Escherichia coli Proteins
- Gene Expression Regulation, Bacterial
- Membrane Transport Proteins
- Models, Molecular
- Mutation
- Protein Binding
- Protein Conformation, alpha-Helical