Rice Science ›› 2026, Vol. 33 ›› Issue (2): 173-185.DOI: 10.1016/j.rsci.2025.11.003
收稿日期:2025-09-24
接受日期:2025-11-25
出版日期:2026-03-28
发布日期:2026-04-01
. [J]. Rice Science, 2026, 33(2): 173-185.
| Tissue/organ | Number of lysine acetylation proteins/sites | Percentage of proteins with multiple lysine acetylation sites (%) | Reference |
|---|---|---|---|
| Suspension cells | 44/60 | 25 | Nallamilli et al, |
| Embryo of seeds | 389/699 | ‒ | He et al, |
| 5-week-old seedlings | 716/1 337 | 39 | Xiong et al, |
| Developing anthers | 676/1 354 | 37 | Li et al, |
| Developing seeds | 692/1 003 | 28 | Meng et al, |
| 3-week-old leaves | 866/1 353 | 31 | Xue et al, |
| 14-day-old leaves | 1 024/1 669 | ‒ | Zhou et al, |
| 14-day-old leaves | 1 952/4 868 | 47 | Xu et al, |
| Crown roots | 2 645/6 099 | 48 | Xu et al, |
Table 1. Lysine acetylomes in different tissues of rice.
| Tissue/organ | Number of lysine acetylation proteins/sites | Percentage of proteins with multiple lysine acetylation sites (%) | Reference |
|---|---|---|---|
| Suspension cells | 44/60 | 25 | Nallamilli et al, |
| Embryo of seeds | 389/699 | ‒ | He et al, |
| 5-week-old seedlings | 716/1 337 | 39 | Xiong et al, |
| Developing anthers | 676/1 354 | 37 | Li et al, |
| Developing seeds | 692/1 003 | 28 | Meng et al, |
| 3-week-old leaves | 866/1 353 | 31 | Xue et al, |
| 14-day-old leaves | 1 024/1 669 | ‒ | Zhou et al, |
| 14-day-old leaves | 1 952/4 868 | 47 | Xu et al, |
| Crown roots | 2 645/6 099 | 48 | Xu et al, |
| HDAC/HAT | Histone modification site | Biological function | Reference |
|---|---|---|---|
| OsHDA701 | H3K9ac | Regulation of immune responses | Chen et al, |
| OsHDA702 | H3K9, K14, K18ac, H4K5, K12, K16ac | Root growth | Chung et al, |
| OsHDA703 | H4K8, K12ac | Brassinosteroid signal transduction, growth, and heading date | Wang et al, |
| OsHDA704 | H4K8ac | Drought stress response | Guo Y L et al, |
| OsHDA705 | H4K8hib | Pathogen immune response | Xu et al, |
| OsHDA706 | H4K5, K8ac | Salt stress response | Liu et al, |
| OsHDA710 | H4K5, K16ac | Response to salt stress | Ullah et al, |
| OsSRT701 | H3K9ac | Seed development | Zhang et al, |
| OsSRT702 | H4K5, K8ac | Regulate immunity | Chen X Y et al, |
| OsHDT702 | H4K5, K16ac | Regulate plant innate immunity | Ding et al, |
| OsGCN5 | H3K18ac, K27ac | ‒ | Xue et al, |
| OsHAG704 | H4K5ac, K16ac | Cell division | Xu et al, |
Table 2. Types of histone modifications regulated by rice histone deacetylases (HDACs)/histone acetyltransferases (HATs).
| HDAC/HAT | Histone modification site | Biological function | Reference |
|---|---|---|---|
| OsHDA701 | H3K9ac | Regulation of immune responses | Chen et al, |
| OsHDA702 | H3K9, K14, K18ac, H4K5, K12, K16ac | Root growth | Chung et al, |
| OsHDA703 | H4K8, K12ac | Brassinosteroid signal transduction, growth, and heading date | Wang et al, |
| OsHDA704 | H4K8ac | Drought stress response | Guo Y L et al, |
| OsHDA705 | H4K8hib | Pathogen immune response | Xu et al, |
| OsHDA706 | H4K5, K8ac | Salt stress response | Liu et al, |
| OsHDA710 | H4K5, K16ac | Response to salt stress | Ullah et al, |
| OsSRT701 | H3K9ac | Seed development | Zhang et al, |
| OsSRT702 | H4K5, K8ac | Regulate immunity | Chen X Y et al, |
| OsHDT702 | H4K5, K16ac | Regulate plant innate immunity | Ding et al, |
| OsGCN5 | H3K18ac, K27ac | ‒ | Xue et al, |
| OsHAG704 | H4K5ac, K16ac | Cell division | Xu et al, |
Fig. 1. Overview of role of rice histone deacetylases involved in environmental stress response and growth through non-histone acetylation. Ac, Acetylation; Ub, Ubiquitination; JA, Jasmonic acid; PK, Pyruvate kinase; ENO1, Enolase1.
| Modifying enzyme type | Enzyme | Non-histone substrate | Function of acetylation | Mechanism of action | Reference |
|---|---|---|---|---|---|
| Deacetylase | OsHDAC1/ OsHDA702 | OsGSK2 | Kinase activity | Control lateral root formation in rice | Hou et al, |
| OsALDH2B1 | Transcriptional activity, protein stability | Responses to salt stress | Wu et al, | ||
| OsHDA705 | OsECT3 | m6A binding activity | Regulate rice cold tolerance | Ma et al, | |
| OsHDA706 | OsLOX14 | Protein stability | Broad-spectrum antiviral immunity | Yang et al, | |
| OsHDA714 | Ribosomal protein | Protein abundance or stability | ‒ | Xu et al, | |
| OsHDA714 | Glycolytic enzyme | Enzyme activity | Confer plant tolerance to heat stress | Chen Z T et al, | |
| OsHDA716 | OsbZIP46 | Transcriptional activity, protein stability | Response to drought stress; repress rice chilling tolerance | b | |
| OsHDT701 | OsRpp30 | ‒ | Broad-spectrum resistance to fungal and bacterial pathogens | Li et al, | |
| OsSRT1 | GAPDH | Transcriptional activity | Repress glycolysis | Zhang et al, | |
| Acetyltransferase | GCN5 | ADA2 | Protein Stability | Metabolic control | Yu et al, |
| N-terminal acetyltransferase | NatA | GLO1/GLO5 | Protein degradation | Promote rice thermoresponsive growth | Li et al, |
| NatA | OsHYPK | Protein level | Coordinate plant development and abiotic stress responses | Gong et al, |
Table 3. Lysine acetylation modification of non-histone proteins in rice.
| Modifying enzyme type | Enzyme | Non-histone substrate | Function of acetylation | Mechanism of action | Reference |
|---|---|---|---|---|---|
| Deacetylase | OsHDAC1/ OsHDA702 | OsGSK2 | Kinase activity | Control lateral root formation in rice | Hou et al, |
| OsALDH2B1 | Transcriptional activity, protein stability | Responses to salt stress | Wu et al, | ||
| OsHDA705 | OsECT3 | m6A binding activity | Regulate rice cold tolerance | Ma et al, | |
| OsHDA706 | OsLOX14 | Protein stability | Broad-spectrum antiviral immunity | Yang et al, | |
| OsHDA714 | Ribosomal protein | Protein abundance or stability | ‒ | Xu et al, | |
| OsHDA714 | Glycolytic enzyme | Enzyme activity | Confer plant tolerance to heat stress | Chen Z T et al, | |
| OsHDA716 | OsbZIP46 | Transcriptional activity, protein stability | Response to drought stress; repress rice chilling tolerance | b | |
| OsHDT701 | OsRpp30 | ‒ | Broad-spectrum resistance to fungal and bacterial pathogens | Li et al, | |
| OsSRT1 | GAPDH | Transcriptional activity | Repress glycolysis | Zhang et al, | |
| Acetyltransferase | GCN5 | ADA2 | Protein Stability | Metabolic control | Yu et al, |
| N-terminal acetyltransferase | NatA | GLO1/GLO5 | Protein degradation | Promote rice thermoresponsive growth | Li et al, |
| NatA | OsHYPK | Protein level | Coordinate plant development and abiotic stress responses | Gong et al, |
Fig. 2. Comparing sites and proteins between acetylation and other modification types. A, Comparison of acetylated and ubiquitinated groups in rice. B, Comparison of acetylated and succinylated groups in rice seeds. C, Comparison of acetylated and succinylated groups under oxidative stress in rice leaves.
Fig. 3. Biological functions of N-terminal acetylation in rice.
| Classification of detection methods | Specific technology | Advantage | Limitation | Trend development |
|---|---|---|---|---|
| Antibody-dependent | Western blot, immunoprecipitation, immunofluorescence | Easy to operate; low cost | Dependence on antibody quality; low throughput; risk of false positives | Improving antibody specificity |
| Antibody-independent (Mass spectrometry-based) | TMT, iTRAQ, SILAC | High throughput; new site discovery; quantitative accuracy | Sample preparation is complex; require advanced data analysis | Single-cell resolution detection; plant system adaptation |
| Cutting-edge technology | Unlabeled single cell detection | Ultra-high sensitivity; spatial resolution | Immature technology; challenges in plant applications | Developing hypersensitive methods; establishing a spatiotemporal dynamic quantitative framework |
Table 4. Comparison of acetylation technologies.
| Classification of detection methods | Specific technology | Advantage | Limitation | Trend development |
|---|---|---|---|---|
| Antibody-dependent | Western blot, immunoprecipitation, immunofluorescence | Easy to operate; low cost | Dependence on antibody quality; low throughput; risk of false positives | Improving antibody specificity |
| Antibody-independent (Mass spectrometry-based) | TMT, iTRAQ, SILAC | High throughput; new site discovery; quantitative accuracy | Sample preparation is complex; require advanced data analysis | Single-cell resolution detection; plant system adaptation |
| Cutting-edge technology | Unlabeled single cell detection | Ultra-high sensitivity; spatial resolution | Immature technology; challenges in plant applications | Developing hypersensitive methods; establishing a spatiotemporal dynamic quantitative framework |
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