MODIFICATION OF THE TRANSCRIPTION FACTOR FOR GLYCINE MAX TO INCREASE AFFINITY TO THE IN SILICO CAAT-MOTIF
Main Article Content
Breeding new varieties of agricultural crops that are resistant to aggressive environmental conditions without reducing productivity is an important and urgent task. Modern methods of genetics and breeding make it possible to cross varieties in order to develop useful qualities and consolidate them in the population, based on genome mapping data with already annotated traits and genes. The literature offers various markers that are associated with the desired properties, such as microsatellite DNA regions (SSRs) and single nucleotide polymorphisms (SNPs), or are its direct initiator. Quantitative trait loci (QTLs) and transcription factors (TFs) are considered as initiators. If QTLs are required to increase the level of expression, then TFs are one of the key mechanisms for solving this problem. The transcription factor NFYC4 annotated in Arabidopsis thaliana plays an important role in the regulation of the plant's immune response to biotic stress and to the increase in the total protein level. For Glycine max, a homologous analogue has been presented that is responsible for the same functions. At this stage, this protein has an index of I1KC24. An increase in the expression of target genes for this protein is an important task. Protein engineering makes it possible to supplement the process of creating new stress-resistant varieties, due to additional modifications of the identified genes that are responsible for the expression of the necessary properties. In this work, one of the strategic approaches is proposed, which consists in increasing the affinity of a transcription factor for its regulatory region in DNA in silico in order to increase expression. An increase in affinity for the CAAT motif was achieved due to the introduction of multiple amino acid substitutions at the binding site for aspartic acid.
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Qi M. QQS orphan gene and its interactor NF-YC4 reduce susceptibility to pathogens and pests / M. Qi, W. Zheng, X. Zhao [et al.] // Plant Biotechnol J. 2019 Jan; 17(1): 252-263. — DOI: 10.1111/pbi.12961. — Epub 2018 Jul 6. PMID: 29878511; PMCID: PMC6330549.
Francois M. Modulating transcription factor activity: Interfering with protein-protein interaction networks / M. Francois, P. Donovan, F. Fontaine // Semin Cell Dev Biol. 2020 Mar; 99: 12-19. — DOI: 10.1016/j.semcdb.2018.07.019. — Epub 2018 Sep 13. PMID: 30172762.
Tang Y. Arabidopsis NF-YCs Mediate the Light-Controlled Hypocotyl Elongation via Modulating Histone Acetylation / Y. Tang, X. Liu, X. Liu [et al.] // Mol Plant. 2017 Feb 13;10(2): 260-273. — DOI: 10.1016/j.molp.2016.11.007. — Epub 2016 Nov 19. PMID: 27876642.
Li L. QQS orphan gene regulates carbon and nitrogen partitioning across species via NF-YC interactions / L. Li, W. Zheng, Y. Zhu [et al.] // Proc Natl Acad Sci USA. 2015 Nov 24;112(47): 14734-9. — DOI: 10.1073/pnas.1514670112. — Epub 2015 Nov 9. PMID: 26554020; PMCID: PMC4664325.
Liu X. The NF-YC-RGL2 module integrates GA and ABA signalling to regulate seed germination in Arabidopsis / X. Liu, P. Hu, M. Huang [et al.] // Nat Commun. 2016 Sep 14;7: 12768. — DOI: 10.1038/ncomms12768. — PMID: 27624486; PMCID: PMC5027291.
Kumimoto R.W. NF-YC3, NF-YC4 and NF-YC9 are required for CONSTANS-mediated, photoperiod-dependent flowering in Arabidopsis thaliana / R.W. Kumimoto, Y. Zhang, N. Siefers [et al.] // Plant J. 2010 Aug;63(3): 379-91. — DOI: 10.1111/j.1365-313X.2010.04247.x. — Epub 2010 May 6. PMID: 20487380
Bezzecchi E. NF-YA Overexpression in Lung Cancer: LUSC / E. Bezzecchi, M. Ronzio, D. Dolfini [et al.] // Genes (Basel). 2019 Nov 17; 10(11):937. — DOI: 10.3390/genes10110937. — PMID: 31744190; PMCID: PMC6895822.
Sinha S. Predicting Protein Function Using Homology-Based Methods / S. Sinha, B. Eisenhaber, A.M. Lynn; ed. by Shanker A. // Bioinformatics: Sequences, Structures, Phylogeny. — Springer, Singapore, 2018. —DOI: 10.1007/978-981-13-1562-6_13
Lin M. New insights into protein-DNA binding specificity from hydrogen bond based comparative study / M. Lin, J.T. Guo // Nucleic Acids Res. 2019 Dec 2;47(21): 11103-11113. — DOI: 10.1093/nar/gkz963. — PMID: 31665426; PMCID: PMC6868434.
Whisstock J.C. Prediction of protein function from protein sequence and structure / J.C. Whisstock, A.M. Lesk // Quarterly Reviews of Biophysics. 36 (3): 307–40. August 2003. — DOI:10.1017/S0033583503003901. — PMID 15029827. S2CID 27123114