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Operon structure and cotranslational subunit association direct protein assembly in bacteria

Science, Nov 6, 2015, Vol.350(6261), pp.678-680 [Peer Reviewed Journal]

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  • Title:
    Operon structure and cotranslational subunit association direct protein assembly in bacteria
  • Author: Yu-Wei, Shieh ; Minguez, Pablo ; Bork, Peer ; Auburger, Josef ; Kramer, Günter ; Bukau, Bernd
  • Found In: Science, Nov 6, 2015, Vol.350(6261), pp.678-680 [Peer Reviewed Journal]
  • Subjects: Protein Synthesis ; Bacteria ; E Coli ; Proteins
  • Language: English
  • Description: 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 Assembly of protein complexes is considered a posttranslational process involving random collision of subunits. We show that within the Escherichia coli cytosol, bacterial luciferase subunits LuxA and LuxB assemble into complexes close to the site of subunit synthesis. Assembly efficiency decreases markedly if subunits are synthesized on separate messenger RNAs from genes integrated at distant chromosomal sites. Subunit assembly...
  • Identifier: ISSN: 00368075 ; E-ISSN: 10959203 ; DOI: 10.1126/science.aac8171

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