Prevalent structural disorder in E. coli and S. cerevisiae proteomes.

TitlePrevalent structural disorder in E. coli and S. cerevisiae proteomes.
Publication TypeJournal Article
Year of Publication2006
AuthorsTompa, P., Z. Dosztányi, and I. Simon
JournalJ Proteome Res
Volume5
Issue8
Pagination1996-2000
Date Published2006 Aug
ISSN1535-3893
KeywordsAlgorithms, Escherichia coli, Escherichia coli Proteins, Genome, Bacterial, Genome, Fungal, Molecular Sequence Data, Protein Conformation, Proteome, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Abstract

Intrinsically unstructured proteins, which exist without a well-defined 3D structure, carry out essential functions 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 expressed proteins. Here, we used two independent bioinformatic predictors, PONDR VSL1, and IUPred, to demonstrate 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 proteome contains three times as much disorder as that of E. coli, with 50-60% of proteins containing at least one long (>30 residues) disordered segment. This evolutionary advance can be explained by the observation that disorder is much higher in Gene Ontology categories related to regulatory, as opposed to metabolic, functions, and also in categories unique to yeast. Thus, protein disorder is a widespread and functionally important phenomenon, which needs to be characterized in full detail for understanding complex organisms at the molecular level.

DOI10.1021/pr0600881
Alternate JournalJ. Proteome Res.
PubMed ID16889422
Grant List067595 / / Wellcome Trust / United Kingdom