Login Register Cart 0
Generic placeholder image

Current Biotechnology

Editor-in-Chief

ISSN (Print): 2211-5501
ISSN (Online): 2211-551X

Back
Journal Home About Journal Editorial Board Journal Insight Current Issue Volumes/Issues
Subscribe
Short Communication

Proteome-Wide Analysis of Protein Disorder in Durum Wheat

Author(s): Mouna Choura*

Volume 12, Issue 2, 2023

Published on: 28 April, 2023

Page: [124 - 128] Pages: 5

DOI: 10.2174/2211550112666230407101119

Price: $65

Abstract

Introduction: Intrinsically Disordered Proteins (IDPs) are natively unstructured proteins. Interestingly, IDPs are ubiquitous and play key roles in cellular and proteins functions. While IDPs are studied in some proteomes, many remain to be uncovered.

Methods: The data were retrieved from MobiDB database version 4. Intrinsic disorder predictions are made with various prediction tools. We focus on IUpred-L predictions.

Results: Here, we have explored the first large-scale study of IDPs in T. turgidum. Additionally, a comparative analysis of T. turgidum and T. aestivum IDPs was performed for highlighting the disorder use in each species. The data indicated that the T.turgidum proteome is significantly more disordered than the T. aestivum proteome. Gene ontology analysis revealed that IDPs in T. turgidum are mainly catalytic and binding proteins involved in regulation of cellular and metabolic processes.

Conclusion: These findings may constitute a starting point for deeper understanding of IDP roles in stress tolerance and the mechanisms underlying the adaptation capacities differences between T. turgidium and related species.

« Previous Next »
Graphical Abstract

[1]
Dunker AK, Brown CJ, Lawson JD, Iakoucheva LM. Obradović Z. Intrinsic disorder and protein function. Biochemistry 2002; 41(21): 6573-82.
[http://dx.doi.org/10.1021/bi012159+] [PMID: 12022860]
[2]
Uversky VN, Dunker AK. Understanding protein non-folding. Biochim Biophys Acta Proteins Proteomics 2010; 1804(6): 1231-64.
[http://dx.doi.org/10.1016/j.bbapap.2010.01.017] [PMID: 20117254]
[3]
Tompa P. Unstructural biology coming of age. Curr Opin Struct Biol 2011; 21(3): 419-25.
[http://dx.doi.org/10.1016/j.sbi.2011.03.012] [PMID: 21514142]
[4]
Pietrosemoli N, García-Martín JA, Solano R, Pazos F. Genome-wide analysis of protein disorder in Arabidopsis thaliana: Implications for plant environmental adaptation. PLoS One 2013; 8(2): e55524.
[http://dx.doi.org/10.1371/journal.pone.0055524] [PMID: 23408995]
[5]
Xue B, Dunker AK, Uversky VN. Orderly order in protein intrinsic disorder distribution: Disorder in 3500 proteomes from viruses and the three domains of life. J Biomol Struct Dyn 2012; 30(2): 137-49.
[http://dx.doi.org/10.1080/07391102.2012.675145] [PMID: 22702725]
[6]
Choura M, Ebel C, Hanin M. Genomic analysis of intrinsically disordered proteins in cereals: From mining to meaning. Gene 2019; 714: 143984.
[http://dx.doi.org/10.1016/j.gene.2019.143984] [PMID: 31330237]
[7]
Choura M, Rebaï A, Hanin M. Proteome-wide analysis of protein disorder in Triticum aestivum and Hordeum vulgare. Comput Biol Chem 2020; 84: 107138.
[http://dx.doi.org/10.1016/j.compbiolchem.2019.107138] [PMID: 31767506]
[8]
Piovesan D, Necci M, Escobedo N, et al. MobiDB: Intrinsically disordered proteins in 2021. Nucleic Acids Res 2021; 49(D1): D361-7.
[http://dx.doi.org/10.1093/nar/gkaa1058] [PMID: 33237329]
[9]
Walsh I, Martin AJM, Di Domenico T, Tosatto SCE. ESpritz: Accurate and fast prediction of protein disorder. Bioinformatics 2012; 28(4): 503-9.
[http://dx.doi.org/10.1093/bioinformatics/btr682] [PMID: 22190692]
[10]
Dosztányi Z, Csizmok V, Tompa P, Simon I. IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 2005; 21(16): 3433-4.
[http://dx.doi.org/10.1093/bioinformatics/bti541] [PMID: 15955779]
[11]
Linding R, Russell RB, Neduva V, Gibson TJ. GlobPlot: exploring protein sequences for globularity and disorder. Nucleic Acids Res 2003; 31(13): 3701-8.
[http://dx.doi.org/10.1093/nar/gkg519] [PMID: 12824398]
[12]
Linding R, Jensen LJ, Diella F, Bork P, Gibson TJ, Russell RB. Protein disorder prediction: Implications for structural proteomics. Structure 2003; 11(11): 1453-9.
[http://dx.doi.org/10.1016/j.str.2003.10.002] [PMID: 14604535]
[13]
Huang D, Sherman BT, Tan Q, et al. The DAVID gene functional classification tool: A novel biological module-centric algorithm to functionally analyze large gene lists. Genome Biol 2007; 8(9): R183.
[http://dx.doi.org/10.1186/gb-2007-8-9-r183] [PMID: 17784955]
[14]
Schad E, Tompa P, Hegyi H. The relationship between proteome size, structural disorder and organism complexity. Genome Biol 2011; 12(12): R120.
[http://dx.doi.org/10.1186/gb-2011-12-12-r120] [PMID: 22182830]
[15]
Choura M, Rebaï A, Brini F. Exploring the intrinsic disorder of the WRKY transcription factor family in the cereals. J Bioinform 2020; 3: 092-104.
[http://dx.doi.org/10.26502/jbsb.5107017]
[16]
Zamora-Briseño JA, Pereira-Santana A, Reyes-Hernández SJ, Cerqueda-García D, Castaño E, Rodríguez-Zapata LC. Towards an understanding of the role of intrinsic protein disorder on plant adaptation to environmental challenges. Cell Stress Chaperones 2021; 26(1): 141-50.
[http://dx.doi.org/10.1007/s12192-020-01162-5] [PMID: 32902806]
[17]
Choura M, Rebaï A, Masmoudi K. Unraveling the WRKY transcription factors network in Arabidopsis thaliana by integrative approach. New Biol 2015; 5: 55-61.
[18]
Choura M, Brini F. WRKYs in Durum wheat: Intrinsic disorder and interactions. New Biol 2022; 12: 116-9.
[19]
Marti J, Slafer GA. Bread and durum wheat yields under a wide range of environmental conditions. Field Crops Res 2014; 156: 258-71.
[http://dx.doi.org/10.1016/j.fcr.2013.10.008]

Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy