Estimating intrinsic structural preferences of de novo emerging random-sequence proteins: is aggregation the main bottleneck?
Present-day proteins are believed to have evolved features to reduce the risk of aggregation. However, proteins can emerge de novo by translation of non-coding DNA segments. In this study we assess the aggregation, disorder and transmembrane propensity of protein sequences generated by translating random nucleotide sequences of varying GC-content. Potential de novo random-sequence proteins translated from regions with GC content between 40% and 60% do not show stronger aggregation propensity than existing ones and exhibit similar tendency to be disordered. We suggest that de novo emerging proteins do not mean an unavoidable aggregation threat to evolving organisms.
Eötvös Loránd University, Institute of Chemistry, Pázmány Péter s. 1/A, H-1117 Budapest, Hungary.
Annamária F
AF
Ángyán
András
A
Perczel
Zoltán
Z
Gáspári
D000818:Animals; D001482:Base Composition; D019143:Evolution, Molecular; D015894:Genome, Human; D006801:Humans; D051379:Mice; D009711:Nucleotides / Q000378:metabolism; D016366:Open Reading Frames; D014176:Protein Biosynthesis; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000235:genetics*; D040901:Proteomics / Q000379:methods; D012333:RNA, Messenger / Q000378:metabolism; D017422:Sequence Analysis, DNA
D009711:Nucleotides; D011506:Proteins; D012333:RNA, Messenger