An unexpected vestigial protein complex reveals the evolutionary origins of an
| Autor: | Lygie, Esquirol, Thomas S, Peat, Matthew, Wilding, Jian-Wei, Liu, Nigel G, French, Carol J, Hartley, Hideki, Onagi, Thomas, Nebl, Christopher J, Easton, Janet, Newman, Colin, Scott |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular Protein Conformation alpha-Helical Genetic Vectors Gene Expression Crystallography X-Ray Amidohydrolases Substrate Specificity Evolution Molecular Bacterial Proteins Catalytic Domain Pseudomonas Operon Escherichia coli Protein Interaction Domains and Motifs Amino Acid Sequence Cloning Molecular Enzyme Inhibitors Sequence Homology Amino Acid Herbicides Triazines Hydrolysis Organophosphates Recombinant Proteins Isoenzymes Kinetics Editors' Picks Highlights Protein Conformation beta-Strand Protein Multimerization Sequence Alignment Protein Binding |
| Zdroj: | The Journal of biological chemistry. 293(20) |
| ISSN: | 1083-351X |
| Popis: | The introduction of manmade chemicals, including the herbicide atrazine, into the environment has led to the emergence of microorganisms with new biodegradation pathways. Esquirol et al. demonstrate that the AtzE enzyme catalyzes a central step in atrazine degradation and that expression of AtzE requires coexpression of the small protein AtzG. Remarkably, AtzG and AtzE appear to have evolved from GatC and GatA, components of an ancient enzyme involved in indirect tRNA aminoacylation, providing an elegant demonstration of metabolic repurposing. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|