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- W3111382272 abstract "Abstract Serine(S)/threonine(T)-glutamine(Q) cluster domains (SCDs), polyglutamine (polyQ) tracts and polyglutamine/asparagine (polyQ/N) tracts are Q-rich motifs found in many proteins. SCDs often are intrinsically disordered regions that mediate protein phosphorylation and protein-protein interactions. PolyQ and polyQ/N tracts are structurally flexible sequences that trigger protein aggregation. We show that four SCDs and three prion-causing Q/N-rich motifs of yeast proteins possess autonomous protein expression-enhancing activities. Comparative Gene Ontology (GO) analyses of the near-complete proteomes of 27 representative model eukaryotes reveal that Q-rich motifs prevail in proteins involved in specialized biological processes, including Saccharomyces cerevisiae RNA-mediated transposition, Candida albicans filamentous growth, ciliate peptidyl-glutamic acid modification, Tetrahymena thermophila xylan catabolism and meiosis, Dictyostelium discoideum development and sexual cycles, Plasmodium falciparum infection, and the Drosophila melanogaster nervous system. We also show that Q-rich motifs are expanded massively in ten ciliates with reassigned TAA Q and TAG Q codons. Our results provide new insights to explain why many ciliates reassign their nuclear stop codons into glutamine (Q). The consequence of this preponderance of Q is massive expansion of proteins harboring three structurally flexible or even intrinsically disordered Q-rich motifs. Since these Q-rich motifs can endow proteins with structural and functional plasticity, we suggest that they represent useful toolkits for evolutionary novelty." @default.
- W3111382272 created "2020-12-21" @default.
- W3111382272 creator A5011795190 @default.
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- W3111382272 creator A5051953260 @default.
- W3111382272 date "2020-12-08" @default.
- W3111382272 modified "2023-09-26" @default.
- W3111382272 title "Intrinsic disorder codes for leaps of protein expression" @default.
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