文摘
Intrinsically unstructured proteins, which exist without a well-defined 3D structure, carry out essentialfunctions and occur with high frequency, as predicted for genomes. The generality of this phenomenon,however, is questioned by the uncertainty of what fraction of genomes actually encodes for expressedproteins. Here, we used two independent bioinformatic predictors, PONDR VSL1, and IUPred, todemonstrate that disorder prevails in the recently characterized proteomes and essential proteins of E.coli and S. cerevisiae, at levels exceeding that estimated from the genomes. The S. cerevisiae proteomecontains three times as much disorder as that of E. coli, with 50-60% of proteins containing at leastone long (>30 residues) disordered segment. This evolutionary advance can be explained by theobservation that disorder is much higher in Gene Ontology categories related to regulatory, as opposedto metabolic, functions, and also in categories unique to yeast. Thus, protein disorder is a widespreadand functionally important phenomenon, which needs to be characterized in full detail for understandingcomplex organisms at the molecular level.