Operon structure and cotranslational subunit association direct protein assembly in bacteria
| Autor: | Günter Kramer, Peer Bork, Pablo Minguez, Bernd Bukau, D. Lys Guilbride, Josef J. Auburger, Yu-Wei Shieh |
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| Rok vydání: | 2015 |
| Předmět: |
Operon
Recombinant Fusion Proteins Protein subunit Green Fluorescent Proteins Ribosome Protein Structure Secondary Protein structure Bacterial Proteins Gene Order Escherichia coli Protein biosynthesis RNA Messenger Vibrio Genetics Multidisciplinary Bacteria biology RNA Cell biology Luciferases Bacterial Luminescent Proteins Protein Subunits Cytosol Genes Bacterial Protein Biosynthesis Chaperone (protein) biology.protein Ribosomes Molecular Chaperones |
| Zdroj: | Science. 350:678-680 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.aac8171 |
| Popis: | Proximity best for building protein complexes The synthesis of protein subunits and their assembly into a fully functional complex are generally thought to be two distinct processes. Shieh et al. studied the synthesis and assembly of the luciferase complex in Escherichia coli. Organization of the luciferase subunits LuxA and LuxB side by side into an operon promotes their colocalized synthesis and assembly into an active enzyme complex. Indeed, the association between the subunits occurs as they are being synthesized on ribosomes, which helps order the sequence of subunit interactions. Science , this issue p. 678 |
| Databáze: | OpenAIRE |
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