Comprehensive Research Report: Functional Annotation of LOC123148885 (Wheat JmjC Domain-Containing Protein) Falcon Edison Scientific Literature 17 citations 1 artifacts 2026-06-18T17:31:32.401003

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Comprehensive Research Report: Functional Annotation of LOC123148885 (Wheat JmjC Domain-Containing Protein)

Gene Identity Verification

LOC123148885 encodes a JmjC domain-containing protein in Triticum aestivum (wheat) that belongs to the JARID1 histone demethylase family (UniProt: A0A3B6RKV1). No direct scientific literature exists specifically for this gene. However, comprehensive genome-wide analyses of the JmjC gene family in wheat and other plants provide substantial functional context for annotation (wang2022genomewideidentificationof pages 1-2, wang2022genomewideidentificationof pages 3-5).

Primary Molecular Function: Histone Demethylation

Enzymatic Activity and Substrate Specificity

The primary function of LOC123148885 can be inferred from its membership in the KDM5/JARID1 subfamily of JmjC domain-containing histone demethylases. This subfamily specifically catalyzes the removal of methyl groups from histone H3 lysine 4 monomethyl, dimethyl, and trimethyl marks (H3K4me1/2/3) (ma2022evolutionaryhistoryand pages 2-3, ma2022evolutionaryhistoryand pages 3-7, viana2025exploringepigeneticmodifiers pages 2-4).

The catalytic mechanism involves Fe(II)- and α-ketoglutarate-dependent oxidative demethylation (ma2022evolutionaryhistoryand pages 1-2, wang2022genomewideidentificationof pages 1-2). The JmjC domain contains highly conserved catalytic residues that coordinate these cofactors: three residues bind Fe(II) (His, Glu/Asp, His) and two residues bind α-ketoglutarate (Thr/Phe, Lys) (ma2022evolutionaryhistoryand pages 3-7). These conserved residues are essential for enzymatic activity, and mutations can significantly affect catalytic function (ma2022evolutionaryhistoryand pages 3-7, yin2024jmjcdomaincontaininghistone pages 2-3).

In wheat, the JmjC gene family was comprehensively characterized by Wang et al. (2022), who identified 24 JmjC genes distributed across two major subfamilies. Of these, 9 members belong to the KDM5/JARID subfamily (designated subfamily II), while 15 belong to the KDM4/JHDM3 subfamily (wang2022genomewideidentificationof pages 3-5). The KDM5/JARID subfamily members can bind and demethylate H3K4 methylation marks at chromatin, thereby regulating gene expression (ma2022evolutionaryhistoryand pages 2-3, wang2022genomewideidentificationof pages 1-2).

Biochemical Context

H3K4 methylation is generally associated with transcriptionally active chromatin and is enriched at gene promoters and regulatory regions (ma2022evolutionaryhistoryand pages 2-3, li2024therolesof pages 2-3). By removing these activating marks, KDM5/JARID1 proteins can repress gene transcription and modulate chromatin accessibility. This demethylation activity is dynamic and reversible, allowing for precise temporal and spatial control of gene expression during development and in response to environmental stimuli (ma2022evolutionaryhistoryand pages 1-2, ma2022evolutionaryhistoryand pages 3-7).

Additional Protein Domains and Potential Functions

F-box Domain

LOC123148885 contains an F-box domain (IPR001810), which is a characteristic feature of F-box proteins that function as substrate recognition subunits within SCF (Skp1-Cullin1-F-box) E3 ubiquitin ligase complexes (saxena2023roleoffbox pages 1-3). F-box proteins recruit specific protein substrates for ubiquitination, marking them for degradation by the 26S proteasome (saxena2023roleoffbox pages 1-3).

The presence of both a JmjC histone demethylase domain and an F-box domain in the same protein is notable and suggests potential dual functionality: (1) direct epigenetic regulation through histone demethylation, and (2) proteolytic regulation through targeted protein degradation. This combination could allow LOC123148885 to coordinate chromatin modification with protein turnover, although the exact protein substrates for the F-box domain remain uncharacterized (saxena2023roleoffbox pages 1-3).

In plants, F-box proteins regulate numerous biological processes including hormone signaling (auxin, jasmonate, gibberellin, ethylene, ABA), developmental transitions, flowering time, and stress responses (saxena2023roleoffbox pages 1-3). The SCF complex machinery is critical for protein quality control and signal transduction in plant cells.

The UniProt annotation indicates similarity to JMJD6 family proteins (IPR050910). In mammalian systems, JMJD6 proteins function primarily as lysine hydroxylases rather than demethylases, catalyzing C5-hydroxylation of lysine residues in unstructured lysine-rich protein domains (cockman2022widespreadhydroxylationof pages 1-2). However, family-level phylogenetic evidence strongly supports LOC123148885 as a KDM5/JARID1-type H3K4 demethylase rather than a JMJD6-type hydroxylase (ma2022evolutionaryhistoryand pages 1-2, wang2022genomewideidentificationof pages 3-5). The JMJD6 annotation likely reflects structural similarity in the JmjC catalytic core rather than functional equivalence.

Subcellular Localization

JmjC domain-containing proteins in wheat are predominantly nuclear. Wang et al. (2022) reported that 18 of 24 wheat JmjC family members are predicted to localize to the nucleus, consistent with their chromatin-associated functions (wang2022genomewideidentificationof pages 3-5). Similarly, in cowpea (Vigna unguiculata), 19 of 26 JMJ proteins were predicted to be nuclear, with minority populations in chloroplast, mitochondria, plasma membrane, and cytoplasm (viana2025exploringepigeneticmodifiers pages 2-4).

Nuclear localization is essential for JARID1 proteins to access their histone substrates on chromatin. The nuclear compartment provides the necessary environment for epigenetic regulation of gene expression through direct interaction with nucleosomes (wang2022genomewideidentificationof pages 3-5).

Biological Processes and Signaling Pathways

Flowering Time Regulation

In model plant species, particularly Arabidopsis thaliana, KDM5/JARID subfamily members play critical roles in flowering time control. For example, AtJMJ15 and AtJMJ18 bind to FLOWERING LOCUS C (FLC) chromatin and reduce H3K4 methylation levels, thereby repressing FLC expression (ma2022evolutionaryhistoryand pages 2-3). This de-repression promotes expression of FLOWERING LOCUS T (FT) in companion cells, accelerating flowering and leading to an early flowering phenotype (ma2022evolutionaryhistoryand pages 2-3).

These findings suggest that wheat JARID1 proteins, including LOC123148885, may similarly regulate flowering-time genes in cereals, coordinating reproductive development with environmental and developmental cues (ma2022evolutionaryhistoryand pages 2-3, ma2022evolutionaryhistoryand pages 3-7).

Abiotic and Biotic Stress Responses

JmjC genes in wheat show dynamic expression patterns in response to drought stress, with distinct temporal phases of regulation (wang2022genomewideidentificationof pages 1-2, wang2022genomewideidentificationof pages 3-5). Analysis of cis-acting regulatory elements in wheat JmjC gene promoters revealed enrichment for hormone-responsive elements including those for abscisic acid (ABA), methyl jasmonate (MeJA), salicylic acid (SA), gibberellin (GA), auxin (IAA), and ethylene (ma2022evolutionaryhistoryand pages 3-7, wang2022genomewideidentificationof pages 3-5).

Wang et al. (2022) demonstrated that certain wheat JmjC members displayed significantly elevated expression after 24 hours of PEG (polyethylene glycol) treatment, indicating roles in the later stages of drought stress response (wang2022genomewideidentificationof pages 1-2, wang2022genomewideidentificationof pages 3-5). Other members showed early induction patterns, suggesting they may be regulated by multiple hormones and function in the early phases of drought stress (wang2022genomewideidentificationof pages 3-5).

In other plant species, JmjC proteins have been shown to regulate stress-responsive gene expression by modulating histone methylation at key loci. For example, overexpression of AtJMJ15 in Arabidopsis confers enhanced salt tolerance (ma2022evolutionaryhistoryand pages 2-3). In rice, JMJ704 suppresses defense responses by reducing H3K4me2/3 levels at defense gene loci (ma2022evolutionaryhistoryand pages 2-3).

Development and Regeneration

Histone H3K4 methylation and demethylation play central roles in plant regeneration and somatic embryogenesis. During dedifferentiation and callus formation, DNA methylation and histone modifications undergo dynamic changes (li2024therolesof pages 2-3). The controlled removal of H3K4 methylation by demethylases is essential for reprogramming cell fate and establishing pluripotency during tissue culture (li2024therolesof pages 2-3).

Reduction of H3K27me3 levels (mediated by other JmjC subfamilies) facilitates initial phases of plant regeneration, where cells dedifferentiate and proliferate. Similar epigenetic dynamics likely extend to H3K4 demethylation, suggesting roles for JARID1 proteins in developmental plasticity and organ regeneration in wheat (li2024therolesof pages 2-3).

Brassinosteroid Signaling and Circadian Rhythms

Plant JmjC proteins are involved in brassinosteroid (BR) signaling pathways, which regulate growth, development, and stress responses (ma2022evolutionaryhistoryand pages 1-2). Some JmjC family members also participate in circadian rhythm regulation, controlling the timing of daily physiological processes (ma2022evolutionaryhistoryand pages 2-3).

Summary of Functional Annotation

Domain Molecular Function Substrate Specificity Subcellular Localization Biological Processes
JmjC domain Fe(II)/α-ketoglutarate-dependent oxidative demethylase catalytic core; in plant KDM5/JARID proteins, inferred to remove activating histone methyl marks and thereby modulate transcription (ma2022evolutionaryhistoryand pages 1-2, ma2022evolutionaryhistoryand pages 3-7, viana2025exploringepigeneticmodifiers pages 2-4) Primarily histone H3 lysine 4 mono-, di-, and trimethylation (H3K4me1/2/3) for the KDM5/JARID subfamily (ma2022evolutionaryhistoryand pages 2-3, ma2022evolutionaryhistoryand pages 3-7, viana2025exploringepigeneticmodifiers pages 2-4) Predominantly nuclear for wheat JmjC proteins; 18 of 24 wheat JmjC family members were predicted nuclear, consistent with chromatin-associated activity (wang2022genomewideidentificationof pages 3-5) Epigenetic regulation of gene expression, chromatin remodeling, flowering control, developmental regulation, and abiotic/biotic stress responses (ma2022evolutionaryhistoryand pages 2-3, wang2022genomewideidentificationof pages 1-2, ma2022evolutionaryhistoryand pages 3-7)
KDM5/JARID family assignment Functional inference that LOC123148885 belongs to the H3K4 demethylase branch of plant JmjC proteins; wheat contains 9 KDM5/JARID members among 24 JmjC genes (wang2022genomewideidentificationof pages 3-5) Active chromatin marks on target loci; likely acts at promoters/gene bodies carrying H3K4 methylation (ma2022evolutionaryhistoryand pages 2-3, wang2022genomewideidentificationof pages 1-2) Expected to function on nuclear chromatin based on family role and wheat JmjC localization patterns (wang2022genomewideidentificationof pages 3-5) Regulation of flowering-time genes such as FLC/FT in model plants; broader transcriptional tuning in growth and stress adaptation in cereals and other plants (ma2022evolutionaryhistoryand pages 2-3, ma2022evolutionaryhistoryand pages 3-7)
Conserved catalytic residues within JmjC core Coordinate Fe(II) and α-ketoglutarate required for oxidative demethylation; conserved His/Glu(or Asp)/His for metal binding and Phe(or Thr)/Lys for cofactor binding in KDM5/JARID proteins (ma2022evolutionaryhistoryand pages 3-7) Enables demethylation chemistry on methyl-lysine substrates; loss/change of these residues can alter or abolish catalytic activity (ma2022evolutionaryhistoryand pages 3-7, yin2024jmjcdomaincontaininghistone pages 2-3) Nuclear if acting on histones; catalytic chemistry itself is domain intrinsic (ma2022evolutionaryhistoryand pages 3-7, wang2022genomewideidentificationof pages 3-5) Supports enzymatic control of transcriptional states through reversible histone methylation (ma2022evolutionaryhistoryand pages 1-2, ma2022evolutionaryhistoryand pages 3-7)
F-box domain / F-box-like domain Putative substrate-recognition module of SCF (Skp1-Cullin1-F-box) E3 ubiquitin ligase complexes; mediates recruitment of specific proteins for ubiquitination and proteasomal turnover (saxena2023roleoffbox pages 1-3) Protein substrates rather than histone methyl marks; exact substrate(s) for LOC123148885 are unknown (saxena2023roleoffbox pages 1-3) Often nuclear and/or cytoplasmic depending on SCF target location; for this wheat chromatin-associated protein, a nuclear role is plausible but unverified (wang2022genomewideidentificationof pages 3-5, saxena2023roleoffbox pages 1-3) Protein turnover, signal transduction, hormone responses, development, and stress adaptation; may couple epigenetic regulation with regulated proteolysis if functional in this protein context (saxena2023roleoffbox pages 1-3)
Cupin_8 / JMJD6_ArgDemeth-LysHydrox-related annotation Suggests structural similarity to 2-oxoglutarate oxygenase folds found in JmjC/JMJD proteins; however, family-level evidence favors histone H3K4 demethylation over assigning JMJD6-like lysine hydroxylase activity to this wheat protein (cockman2022widespreadhydroxylationof pages 1-2, ma2022evolutionaryhistoryand pages 1-2) JMJD6-like proteins in animals can hydroxylate lysine-rich regions, but this activity is not established for LOC123148885; substrate assignment for this wheat protein should remain H3K4me1/2/3 by KDM5-family inference (cockman2022widespreadhydroxylationof pages 1-2, ma2022evolutionaryhistoryand pages 1-2) Likely nuclear because the dominant evidence supports chromatin-associated function in plants (wang2022genomewideidentificationof pages 3-5) Conservative annotation supports chromatin regulation rather than direct assignment to non-histone hydroxylation pathways (ma2022evolutionaryhistoryand pages 1-2, cockman2022widespreadhydroxylationof pages 1-2)
Whole-protein functional annotation for LOC123148885 Putative chromatin-associated epigenetic regulator in wheat combining a JARID1/KDM5-type histone demethylase core with an F-box-related module; best-supported primary function is transcriptional regulation via H3K4 demethylation (ma2022evolutionaryhistoryand pages 1-2, wang2022genomewideidentificationof pages 3-5, saxena2023roleoffbox pages 1-3) Most likely H3K4me1/2/3 on histone H3; precise gene targets in wheat remain uncharacterized (ma2022evolutionaryhistoryand pages 2-3, wang2022genomewideidentificationof pages 1-2, wang2022genomewideidentificationof pages 3-5) Most likely nucleus (family-level prediction and wheat JmjC localization trend) (wang2022genomewideidentificationof pages 3-5) Likely involved in developmental timing, hormone/stress-responsive transcription, and possibly drought-related regulation, based on wheat JmjC family expression and plant KDM5 biology (wang2022genomewideidentificationof pages 1-2, wang2022genomewideidentificationof pages 3-5)

Table: This table summarizes the inferred functional annotation of the wheat protein LOC123148885 based on its domain architecture and the known biology of plant JmjC/KDM5(JARID1) proteins. It is useful because direct literature on this specific wheat gene is limited, so the most reliable interpretation comes from domain- and family-level evidence.

Evidence Basis and Limitations

The functional annotation of LOC123148885 is based primarily on domain architecture analysis and inference from extensively characterized JmjC/JARID1 family members in wheat and other plant species. Key supporting evidence includes:

  1. Genome-wide characterization of wheat JmjC family (Wang et al. 2022) identified 9 KDM5/JARID subfamily members with conserved domain structure and nuclear localization (wang2022genomewideidentificationof pages 1-2, wang2022genomewideidentificationof pages 3-5)

  2. Phylogenetic and evolutionary analyses across 21 plant species confirmed that KDM5/JARID subfamily members specifically demethylate H3K4me1/2/3 marks (ma2022evolutionaryhistoryand pages 1-2, ma2022evolutionaryhistoryand pages 3-7)

  3. Functional studies in model plants (Arabidopsis, rice, tomato) demonstrated roles in flowering, stress responses, and development through H3K4 demethylation (ma2022evolutionaryhistoryand pages 2-3, wang2022genomewideidentificationof pages 1-2)

  4. Biochemical characterization of conserved catalytic residues and cofactor requirements (Fe(II), α-ketoglutarate) for JmjC-mediated demethylation (ma2022evolutionaryhistoryand pages 1-2, ma2022evolutionaryhistoryand pages 3-7)

Limitations: Direct experimental validation of LOC123148885 function in wheat has not been published. The specific gene targets, protein interaction partners, and physiological roles in wheat development and stress adaptation remain to be determined through functional genomics approaches.

Research and Biotechnology Implications

Understanding the function of LOC123148885 and other wheat JARID1 proteins has significant implications for crop improvement. Epigenetic regulation of flowering time, stress tolerance, and developmental plasticity are critical agronomic traits. Targeted manipulation of histone demethylases could provide strategies for:

  1. Optimizing flowering time for specific growing environments
  2. Enhancing drought tolerance and abiotic stress resilience
  3. Improving regeneration efficiency in tissue culture and transformation protocols
  4. Fine-tuning gene expression for yield optimization

Future research should focus on characterizing the specific chromatin targets of LOC123148885, identifying protein interaction partners (especially for the F-box domain), and evaluating phenotypes of knockout or overexpression lines in wheat under diverse environmental conditions.

References

This report is based on peer-reviewed scientific literature published between 2020-2025, with emphasis on recent genome-wide characterizations and functional studies of JmjC domain-containing proteins in plants. Citations are provided in the context ID format (pqac-########) throughout the text.

References

  1. (wang2022genomewideidentificationof pages 1-2): Xinhua Wang, Cuili Pan, Jiaohui Long, Shuangyu Bai, Mingming Yao, Jiajing Chen, Gang Sun, Yalei Fan, Zhangjun Wang, Fenglou Liu, Caixia Liu, and Qingfeng Li. Genome-wide identification of the jumonji c domain- containing histone demethylase gene family in wheat and their expression analysis under drought stress. Frontiers in Plant Science, Aug 2022. URL: https://doi.org/10.3389/fpls.2022.987257, doi:10.3389/fpls.2022.987257. This article has 17 citations.

  2. (wang2022genomewideidentificationof pages 3-5): Xinhua Wang, Cuili Pan, Jiaohui Long, Shuangyu Bai, Mingming Yao, Jiajing Chen, Gang Sun, Yalei Fan, Zhangjun Wang, Fenglou Liu, Caixia Liu, and Qingfeng Li. Genome-wide identification of the jumonji c domain- containing histone demethylase gene family in wheat and their expression analysis under drought stress. Frontiers in Plant Science, Aug 2022. URL: https://doi.org/10.3389/fpls.2022.987257, doi:10.3389/fpls.2022.987257. This article has 17 citations.

  3. (ma2022evolutionaryhistoryand pages 2-3): Shifeng Ma, Zhiqiang Zhang, Yingqiang Long, Wenqi Huo, Yuzhi Zhang, Xiaoqing Yang, Jie Zhang, Xinyang Li, Qiying Du, Wei Liu, Daigang Yang, and Xiongfeng Ma. Evolutionary history and functional diversification of the jmjc domain-containing histone demethylase gene family in plants. Plants, 11:1041, Apr 2022. URL: https://doi.org/10.3390/plants11081041, doi:10.3390/plants11081041. This article has 20 citations.

  4. (ma2022evolutionaryhistoryand pages 3-7): Shifeng Ma, Zhiqiang Zhang, Yingqiang Long, Wenqi Huo, Yuzhi Zhang, Xiaoqing Yang, Jie Zhang, Xinyang Li, Qiying Du, Wei Liu, Daigang Yang, and Xiongfeng Ma. Evolutionary history and functional diversification of the jmjc domain-containing histone demethylase gene family in plants. Plants, 11:1041, Apr 2022. URL: https://doi.org/10.3390/plants11081041, doi:10.3390/plants11081041. This article has 20 citations.

  5. (viana2025exploringepigeneticmodifiers pages 2-4): Jéssica Barbara Vieira Viana, José Ribamar Costa Ferreira-Neto, Eliseu Binneck, Roberta Lane de Oliveira Silva, Antônio Félix da Costa, and Ana Maria Benko-Iseppon. Exploring epigenetic modifiers in cowpea: genomic and transcriptomic insights into histone methyltransferases and histone demethylases. Stresses, 5:13, Feb 2025. URL: https://doi.org/10.3390/stresses5010013, doi:10.3390/stresses5010013. This article has 1 citations.

  6. (ma2022evolutionaryhistoryand pages 1-2): Shifeng Ma, Zhiqiang Zhang, Yingqiang Long, Wenqi Huo, Yuzhi Zhang, Xiaoqing Yang, Jie Zhang, Xinyang Li, Qiying Du, Wei Liu, Daigang Yang, and Xiongfeng Ma. Evolutionary history and functional diversification of the jmjc domain-containing histone demethylase gene family in plants. Plants, 11:1041, Apr 2022. URL: https://doi.org/10.3390/plants11081041, doi:10.3390/plants11081041. This article has 20 citations.

  7. (yin2024jmjcdomaincontaininghistone pages 2-3): Fengrui Yin, Yuanfeng Hu, Xiaoqun Cao, Xufeng Xiao, Ming Zhang, Yan Xiang, Liangdeng Wang, Yuekeng Yao, Meilan Sui, and Wenling Shi. Jmjc domain-containing histone demethylase gene family in chinese cabbage: genome-wide identification and expressional profiling. PLOS ONE, 19:e0312798, Nov 2024. URL: https://doi.org/10.1371/journal.pone.0312798, doi:10.1371/journal.pone.0312798. This article has 5 citations and is from a peer-reviewed journal.

  8. (li2024therolesof pages 2-3): Jiawen Li, Qiyan Zhang, Zejia Wang, and Qikun Liu. The roles of epigenetic regulators in plant regeneration: exploring patterns amidst complex conditions. Plant Physiology, 194:2022-2038, Jan 2024. URL: https://doi.org/10.1093/plphys/kiae042, doi:10.1093/plphys/kiae042. This article has 36 citations and is from a highest quality peer-reviewed journal.

  9. (saxena2023roleoffbox pages 1-3): Harshita Saxena, Harshita Negi, and Bhaskar Sharma. Role of f-box e3-ubiquitin ligases in plant development and stress responses. Plant Cell Reports, 42:1133-1146, May 2023. URL: https://doi.org/10.1007/s00299-023-03023-8, doi:10.1007/s00299-023-03023-8. This article has 59 citations and is from a peer-reviewed journal.

  10. (cockman2022widespreadhydroxylationof pages 1-2): Matthew E. Cockman, Yoichiro Sugimoto, Hamish B. Pegg, Norma Masson, Eidarus Salah, Anthony Tumber, Helen R. Flynn, Joanna M. Kirkpatrick, Christopher J. Schofield, and Peter J. Ratcliffe. Widespread hydroxylation of unstructured lysine-rich protein domains by jmjd6. Proceedings of the National Academy of Sciences of the United States of America, Aug 2022. URL: https://doi.org/10.1073/pnas.2201483119, doi:10.1073/pnas.2201483119. This article has 33 citations and is from a highest quality peer-reviewed journal.

Artifacts

Citations

  1. ma2022evolutionaryhistoryand pages 3-7
  2. wang2022genomewideidentificationof pages 3-5
  3. saxena2023roleoffbox pages 1-3
  4. cockman2022widespreadhydroxylationof pages 1-2
  5. viana2025exploringepigeneticmodifiers pages 2-4
  6. ma2022evolutionaryhistoryand pages 2-3
  7. li2024therolesof pages 2-3
  8. ma2022evolutionaryhistoryand pages 1-2
  9. wang2022genomewideidentificationof pages 1-2
  10. yin2024jmjcdomaincontaininghistone pages 2-3
  11. https://doi.org/10.3389/fpls.2022.987257,
  12. https://doi.org/10.3390/plants11081041,
  13. https://doi.org/10.3390/stresses5010013,
  14. https://doi.org/10.1371/journal.pone.0312798,
  15. https://doi.org/10.1093/plphys/kiae042,
  16. https://doi.org/10.1007/s00299-023-03023-8,
  17. https://doi.org/10.1073/pnas.2201483119,