Conservation of intrinsic disorder in protein domains and families

II. Functions of conserved disorder

Jessica Walton Chen, Pedro Romero, Vladimir N. Uversky, A. Dunker

Research output: Contribution to journalArticle

84 Citations (Scopus)

Abstract

Regions of conserved disorder prediction (CDP) were found in protein domains from all available InterPro member databases, although with varying frequency. These CDP regions were found in proteins from all kingdoms of life, including viruses. However, eukaryotes had 1 order of magnitude more proteins containing long disordered regions than did archaea and bacteria. Sequence conservation in CDP regions varied, but was on average slightly lower than in regions of conserved order. In some cases, disordered regions evolve faster than ordered regions, in others they evolve slower, and in the rest they evolve at roughly the same rate. A variety of functions were found to be associated with domains containing conserved disorder. The most common were DNA/RNA binding, and protein binding. Many ribosomal proteins also were found to contain conserved disordered regions. Other functions identified included membrane translocation and amino acid storage for germination. Due to limitations of current knowledge as well as the methodology used for this work, it was not determined whether these functions were directly associated with the predicted disordered region. However, the functions associated with conserved disorder in this work are in agreement with the functions found in other studies to correlate to disordered regions. We have established that intrinsic disorder may be more common in bacterial and archaeal proteins than previously thought, but this disorder is likely to be used for different purposes than in eukaryotic proteins, as well as occurring in shorter stretches of protein. Regions of predicted disorder were found to be conserved within a large number of protein families and domains. Although many think of such conserved domains as being ordered, in fact a significant number of them contain regions of disorder that are likely to be crucial to their functions.

Original languageEnglish
Pages (from-to)888-898
Number of pages11
JournalJournal of Proteome Research
Volume5
Issue number4
DOIs
StatePublished - Apr 2006

Fingerprint

Conservation
Proteins
Archaeal Proteins
RNA-Binding Proteins
Bacterial Proteins
Ribosomal Proteins
Archaea
DNA-Binding Proteins
Germination
Eukaryota
Protein Binding
Databases
Viruses
Bacteria
Amino Acids
Membranes
Protein Domains
DNA

Keywords

  • Disorder prediction
  • Intrinsic disorder
  • PONDR
  • Protein structure-function

ASJC Scopus subject areas

  • Genetics
  • Biotechnology
  • Biochemistry

Cite this

Conservation of intrinsic disorder in protein domains and families : II. Functions of conserved disorder. / Chen, Jessica Walton; Romero, Pedro; Uversky, Vladimir N.; Dunker, A.

In: Journal of Proteome Research, Vol. 5, No. 4, 04.2006, p. 888-898.

Research output: Contribution to journalArticle

Chen, Jessica Walton ; Romero, Pedro ; Uversky, Vladimir N. ; Dunker, A. / Conservation of intrinsic disorder in protein domains and families : II. Functions of conserved disorder. In: Journal of Proteome Research. 2006 ; Vol. 5, No. 4. pp. 888-898.
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