Extended Data Fig. 3: Cotranslational assembly of the anthranilate synthase complex.
From: Cotranslational assembly of protein complexes in eukaryotes revealed by ribosome profiling
a, Domain organization of the anthranilate synthase subunits. b, Engagement of nascent Trp2p (tryptophan 2) and Trp3p (tryptophan 3) by C-terminally-tagged Trp2p subunit (top) compared to engagement of nascent Trp2p and Trp3p by C-terminally-tagged Trp3p subunit (bottom), analysed by SeRP. Data are from two biologically independent experiments. Coloured numbers indicate ribosome positions where the enrichment stably crosses the twofold threshold. The area between replicates is shaded, indicating the degree of experimental variation. c, Crystal structure of the homologous anthranilate synthase complex from the archaea Sulfolobus solfataricus (~60% sequence similarity, PDB: 1QDL1). d, GFP tagging of the complex subunits does not affect cell growth under tryptophan depletion conditions (YPD, right panel compared to SD lacking tryptophan, left). A representative image from three biologically independent experiments is shown. e, Model of the anthranilate synthase assembly pathway.
