Identification of Intrinsically Disordered Proteins and Regions in a Non-Model Insect Species Ostrinia nubilalis (Hbn.)

Research in previous decades has shown that intrinsically disordered proteins (IDPs) and regions in proteins (IDRs) are as ubiquitous as highly ordered proteins. Despite this, research on IDPs and IDRs still has many gaps left to fill. Here, we present an approach that combines wet lab methods with...

Full description

Saved in:
Bibliographic Details
Published in:Biomolecules (Basel, Switzerland) Switzerland), 2022-04, Vol.12 (4), p.592
Main Authors: Avramov, Miloš, Schád, Éva, Révész, Ágnes, Turiák, Lilla, Uzelac, Iva, Tantos, Ágnes, Drahos, László, Popović, Željko D
Format: Article
Language:English
Subjects:
Adaptation
Amino acid composition
Animals
Bioinformatics
Cell cycle
Cold
cold hardiness
Cytoskeleton
Insecta - metabolism
intrinsically disordered protein regions (IDRs)
intrinsically disordered proteins (IDPs)
Intrinsically Disordered Proteins - chemistry
IUPred analysis
LC–MS/MS
Ostrinia nubilalis
Protein Conformation
Proteins
Proteomics
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Research in previous decades has shown that intrinsically disordered proteins (IDPs) and regions in proteins (IDRs) are as ubiquitous as highly ordered proteins. Despite this, research on IDPs and IDRs still has many gaps left to fill. Here, we present an approach that combines wet lab methods with bioinformatics tools to identify and analyze intrinsically disordered proteins in a non-model insect species that is cold-hardy. Due to their known resilience to the effects of extreme temperatures, these proteins likely play important roles in this insect's adaptive mechanisms to sub-zero temperatures. The approach involves IDP enrichment by sample heating and double-digestion of proteins, followed by peptide and protein identification. Next, proteins are bioinformatically analyzed for disorder content, presence of long disordered regions, amino acid composition, and processes they are involved in. Finally, IDP detection is validated with an in-house 2D PAGE. In total, 608 unique proteins were identified, with 39 being mostly disordered, 100 partially disordered, 95 nearly ordered, and 374 ordered. One-third contain at least one long disordered segment. Functional information was available for only 90 proteins with intrinsic disorders out of 312 characterized proteins. Around half of the 90 proteins are cytoskeletal elements or involved in translational processes.
ISSN:2218-273X
2218-273X
DOI:10.3390/biom12040592