title: Cotranslational assembly of the yeast SET1C histone methyltransferase complex.
abstract: While probing the role of RNA for the function of SET1C/COMPASS histone methyltransferase, we identified SET1RC (SET1 mRNA-associated complex), a complex that contains SET1 mRNA and Set1, Swd1, Spp1 and Shg1, four of the eight polypeptides that constitute SET1C. Characterization of SET1RC showed that SET1 mRNA binding did not require associated Swd1, Spp1 and Shg1 proteins or RNA recognition motifs present in Set1. RNA binding was not observed when Set1 protein and SET1 mRNA were derived from independent genes or when SET1 transcripts were restricted to the nucleus. Importantly, the protein-RNA interaction was sensitive to EDTA, to the translation elongation inhibitor puromycin and to the inhibition of translation initiation in prt1-1 mutants. Taken together, our results support the idea that SET1 mRNA binding was dependent on translation and that SET1RC assembled on nascent Set1 in a cotranslational manner. Moreover, we show that cellular accumulation of Set1 is limited by the availability of certain SET1C components, such as Swd1 and Swd3, and suggest that cotranslational protein interactions may exert an effect in the protection of nascent Set1 from degradation.
authors.affiliation: Institute of Molecular Biology, University of Zürich, Zürich, Switzerland.
authors.forename: André
authors.initials: A
authors.lastname: Halbach
authors.forename: Haidi
authors.initials: H
authors.lastname: Zhang
authors.forename: Agnieszka
authors.initials: A
authors.lastname: Wengi
authors.forename: Zofia
authors.initials: Z
authors.lastname: Jablonska
authors.forename: Isabel M L
authors.initials: IM
authors.lastname: Gruber
authors.forename: Regula E
authors.initials: RE
authors.lastname: Halbeisen
authors.forename: Pierre-Marie
authors.initials: PM
authors.lastname: Dehé
authors.forename: Patrick
authors.initials: P
authors.lastname: Kemmeren
authors.forename: Frank
authors.initials: F
authors.lastname: Holstege
authors.forename: Vincent
authors.initials: V
authors.lastname: Géli
authors.forename: André P
authors.initials: AP
authors.lastname: Gerber
authors.forename: Bernhard
authors.initials: B
authors.lastname: Dichtl
mesh_terms: D004268:DNA-Binding Proteins / Q000378:metabolism; D004492:Edetic Acid / Q000378:metabolism; D015966:Gene Expression Regulation, Fungal; D011495:Histone-Lysine N-Methyltransferase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D014176:Protein Biosynthesis; D017434:Protein Structure, Tertiary; D011500:Protein Synthesis Inhibitors / Q000378:metabolism; D011691:Puromycin / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D004268:DNA-Binding Proteins; D011500:Protein Synthesis Inhibitors; D012333:RNA, Messenger; C524367:SPP1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; C544604:Shg1 protein, S cerevisiae; C544603:Swd1 protein, S cerevisiae; C544605:Swd3 protein, S cerevisiae; D011691:Puromycin; D004492:Edetic Acid; D011495:Histone-Lysine N-Methyltransferase; C411250:SET1 protein, S cerevisiae