Long indels are disordered: a study of disorder and indels in homologous eukaryotic proteins
| Autor: | Diana Ekman, Sara Light, Rauan Sagit, Arne Elofsson |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Protein family
Biophysics Sequence alignment Biology Biochemistry Analytical Chemistry 03 medical and health sciences INDEL Mutation Homologous chromosome Indel protein structure Molecular Biology 030304 developmental biology Genetics Bioinformatics (Computational Biology) 0303 health sciences Rna processing Intrinsically disordered Point mutation 030302 biochemistry & molecular biology food and beverages Proteins Translation (biology) Evolutionary biology Bioinformatik (beräkningsbiologi) Protein evolution protein |
| Zdroj: | Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics; Vol 1834 |
| ISSN: | 0006-3002 |
| Popis: | Proteins evolve through point mutations as well as by insertions and deletions (indels). During the last decade it has become apparent that protein regions that do not fold into three-dimensional structures, i.e. intrinsically disordered regions, are quite common. Here, we have studied the relationship between protein disorder and indels using HMM-HMM pairwise alignments in two sets of orthologous eukaryotic protein pairs. First, we show that disordered residues are much more frequent among indel residues than among aligned residues and, also are more prevalent among indels than in coils. Second, we observed that disordered residues are particularly common in longer indels. Disordered indels of short-to-medium size are prevalent in the non-terminal regions of proteins while the longest indels, ordered and disordered alike, occur toward the termini of the proteins where new structural units are comparatively well tolerated. Finally, while disordered regions often evolve faster than ordered regions and disorder is common in indels, there are some previously recognized protein families where the disordered region is more conserved than the ordered region. We find that these rare proteins are often involved in information processes, such as RNA processing and translation. This article is part of a Special Issue entitled: The emerging dynamic view of proteins: Protein plasticity in allostery, evolution and self-assembly. GeneFun Project, contract no: LSHG-CT-2004-503567 EDICT project, contract no: FP7-HEALTH-F4-2007-201924 |
| Databáze: | OpenAIRE |
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