Intrinsic structural disorder of DF31, a Drosophila protein of chromatin decondensation and remodeling activities.

TitleIntrinsic structural disorder of DF31, a Drosophila protein of chromatin decondensation and remodeling activities.
Publication TypeJournal Article
Year of Publication2008
AuthorsSzollosi, E., M. Bokor, A. Bodor, A. Perczel, E. Klement, K. F. Medzihradszky, K. Tompa, and P. Tompa
JournalJ Proteome Res
Volume7
Issue6
Pagination2291-9
Date Published2008 Jun
Type of Articleidp
ISSN1535-3893
KeywordsAnimals, Calorimetry, Differential Scanning, Chromatography, Gel, Chromosomal Proteins, Non-Histone, Circular Dichroism, Computational Biology, Cross-Linking Reagents, Drosophila Proteins, Electrophoresis, Gel, Two-Dimensional, Hot Temperature, Hydrophobic and Hydrophilic Interactions, Magnetic Resonance Spectroscopy, Peptide Hydrolases, Protein Conformation, Protein Denaturation, Static Electricity, Tandem Mass Spectrometry
Abstract

Protein disorder is predicted to be widespread in eukaryotic proteomes, although direct experimental evidence is rather limited so far. To fill this gap and to unveil the identity of novel intrinsically disordered proteins (IDPs), proteomic methods that combine 2D electrophoresis with mass spectrometry have been developed. Here, we applied the method developed in our laboratory [ Csizmok et al., Mol. Cell. Proteomics 2006, 5, 265- 273 ] to the proteome of Drosophila melanogaster. Protein Df31, earlier described as a histone chaperone involved in chromatin decondensation and stabilization, was among the IDPs identified. Despite some hints at the unusual structural behavior of Df31, this protein has not yet been structurally characterized. Here, we provide evidence by a variety of techniques such as CD, NMR, gel-filtration, limited proteolyzsis and bioinformatics that Df31 is intrinsically disordered along its entire length. Further, by chemical cross-linking, we provide evidence that it is a monomeric protein, and suggest that its function(s) may benefit from having an extended and highly flexible structural state. The potential functional advantages and the generality of protein disorder among chromatin organizing proteins are discussed in detail. Finally, we also would like to point out the utility of our 2DE/MS technique for discoveringor, as a matter of fact, rediscoveringIDPs even from the complicated proteome of an advanced eukaryote.

DOI10.1021/pr700720c
Alternate JournalJ. Proteome Res.
PubMed ID18484763
Grant ListISRF 067595 / / Wellcome Trust / United Kingdom