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Co-translational control of protein complex formation: a fundamental pathway of cellular organization?
journal contribution
posted on 2018-02-06, 00:00 authored by Neal Williams, Bernhard DichtlBernhard DichtlAnalyses of proteomes from a large number of organisms throughout the domains of life highlight the key role played by multiprotein complexes for the implementation of cellular function. While the occurrence of multiprotein assemblies is ubiquitous, the understanding of pathways that dictate the formation of quaternary structure remains enigmatic. Interestingly, there are now well-established examples of protein complexes that are assembled co-translationally in both prokaryotes and eukaryotes, and indications are that the phenomenon is widespread in cells. Here, we review complex assembly with an emphasis on co-translational pathways, which involve interactions of nascent chains with other nascent or mature partner proteins, respectively. In prokaryotes, such interactions are promoted by the polycistronic arrangement of mRNA and the associated co-translation of functionally related cell constituents in order to enhance otherwise diffusion-dependent processes. Beyond merely stochastic events, however, co-translational complex formation may be sensitive to subunit availability and allow for overall regulation of the assembly process. We speculate how co-translational pathways may constitute integral components of quality control systems to ensure the correct and complete formation of hundreds of heterogeneous assemblies in a single cell. Coupling of folding of intrinsically disordered domains with co-translational interaction of binding partners may furthermore enhance the efficiency and fidelity with which correct conformation is attained. Co-translational complex formation may constitute a fundamental pathway of cellular organization, with profound importance for health and disease.
History
Journal
Biochemical Society transactionsVolume
46Issue
1Pagination
197 - 206Publisher
Portland PressLocation
London, Eng.Publisher DOI
ISSN
0300-5127eISSN
1470-8752Language
engPublication classification
C Journal article; C1 Refereed article in a scholarly journalCopyright notice
2018, The Author(s)Usage metrics
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No categories selectedKeywords
co-translational interactionsintrinsically disordered proteinsmultiprotein complexesprotein–protein interactionquality controlsurveillanceScience & TechnologyLife Sciences & BiomedicineBiochemistry & Molecular BiologyINTRINSICALLY DISORDERED PROTEINHISTONE-3 LYSINE-4 METHYLATIONMESSENGER-RNASACCHAROMYCES-CEREVISIAEQUALITY-CONTROLCOTRANSLATIONAL UBIQUITINATIONGENE-EXPRESSIONPHOTOSYSTEM-IISET1 COMPLEXBINDING
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