Operon structure and cotranslational subunit association direct protein assembly in bacteria

Author:

Shieh Yu-Wei1,Minguez Pablo2,Bork Peer23,Auburger Josef J.1,Guilbride D. Lys14,Kramer Günter1,Bukau Bernd1

Affiliation:

1. Center for Molecular Biology of the University of Heidelberg (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany.

2. European Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, 69117 Heidelberg, Germany.

3. Max-Delbrück-Centre for Molecular Medicine, Robert-Rössle-Strasse 10, 13125 Berlin, Germany.

4. Malaria Research Foundation, Post Office Box 10420, Aspen, CO 81612, USA.

Abstract

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

Funder

German Science Foundation

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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