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| Natura: | Artículo científico |
| Lingua: | en |
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Marine life science & technology
2026
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| Accesso online: | https://pubmed.ncbi.nlm.nih.gov/42186570/ |
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| _version_ | 1868266044096774144 |
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| author | Wei, Fan Pan, Bo Han, Xiangning Al-Farraj, Saleh A Sui, Jianxin Gao, Shan |
| author_facet | Wei, Fan Pan, Bo Han, Xiangning Al-Farraj, Saleh A Sui, Jianxin Gao, Shan Wei, Fan Pan, Bo Han, Xiangning Al-Farraj, Saleh A Sui, Jianxin Gao, Shan |
| collection | PubMed - marine biology |
| contents | Specific tracking of N-terminal clipping on histone H3 in enabled by a custom branched-peptide antibody. Wei, Fan Pan, Bo Han, Xiangning Al-Farraj, Saleh A Sui, Jianxin Gao, Shan Histone H3 clipping, a unique but evolutionarily conserved post-translational modification that irreversibly removes the N-terminal tail of H3, has been reported across diverse eukaryotic lineages. In , a ciliate with nuclear dimorphism, H3 clipping is a proteolytic event generating H3 (H3-Fast) by removing the first six N-terminal amino acids, specifically in the transcriptionally silent micronucleus (MIC). However, the detection of H3 remains technically demanding, time-consuming, and lacks spatio-temporal resolution. To overcome this, a 2 × branched peptide antigen was developed to generate a high-specificity antibody that exclusively recognizes H3, effectively distinguishing it from full-length H3 and other truncation variants. This antibody eliminated the need for labor-intensive MIC isolation and histone extraction, enabling rapid, small-scale detection directly from whole-cell lysates. Using this antibody, dynamic subcellular localization of H3 was investigated through different cell stages, revealing its persistence during vegetation, starvation and early conjugation. However, H3 disappeared concurrently with macronuclear anlage formation, supporting the notation that removal of H3 is a prerequisite for the new macronucleus development. Comparative analyses further revealed that H3 Ser10 phosphorylation, though previously used as an alternative H3 marker, actually occurs strictly after clipping, refining the temporal hierarchy of these two chromatin events. This work provides the first in situ, high-resolution method to track endogenous H3 clipping, providing both a technical platform and new biological insight into the developmental regulation of proteolytic histone modifications. The online version contains supplementary material available at 10.1007/s42995-025-00351-4. |
| format | Artículo científico |
| id | pubmed_42186570 |
| institution | PubMed |
| language | en |
| publishDate | 2026 |
| publisher | Marine life science & technology |
| record_format | pubmed |
| spellingShingle | Specific tracking of N-terminal clipping on histone H3 in enabled by a custom branched-peptide antibody. Wei, Fan Pan, Bo Han, Xiangning Al-Farraj, Saleh A Sui, Jianxin Gao, Shan Specific tracking of N-terminal clipping on histone H3 in enabled by a custom branched-peptide antibody. Wei, Fan Pan, Bo Han, Xiangning Al-Farraj, Saleh A Sui, Jianxin Gao, Shan Histone H3 clipping, a unique but evolutionarily conserved post-translational modification that irreversibly removes the N-terminal tail of H3, has been reported across diverse eukaryotic lineages. In , a ciliate with nuclear dimorphism, H3 clipping is a proteolytic event generating H3 (H3-Fast) by removing the first six N-terminal amino acids, specifically in the transcriptionally silent micronucleus (MIC). However, the detection of H3 remains technically demanding, time-consuming, and lacks spatio-temporal resolution. To overcome this, a 2 × branched peptide antigen was developed to generate a high-specificity antibody that exclusively recognizes H3, effectively distinguishing it from full-length H3 and other truncation variants. This antibody eliminated the need for labor-intensive MIC isolation and histone extraction, enabling rapid, small-scale detection directly from whole-cell lysates. Using this antibody, dynamic subcellular localization of H3 was investigated through different cell stages, revealing its persistence during vegetation, starvation and early conjugation. However, H3 disappeared concurrently with macronuclear anlage formation, supporting the notation that removal of H3 is a prerequisite for the new macronucleus development. Comparative analyses further revealed that H3 Ser10 phosphorylation, though previously used as an alternative H3 marker, actually occurs strictly after clipping, refining the temporal hierarchy of these two chromatin events. This work provides the first in situ, high-resolution method to track endogenous H3 clipping, providing both a technical platform and new biological insight into the developmental regulation of proteolytic histone modifications. The online version contains supplementary material available at 10.1007/s42995-025-00351-4. |
| title | Specific tracking of N-terminal clipping on histone H3 in enabled by a custom branched-peptide antibody. |
| url | https://pubmed.ncbi.nlm.nih.gov/42186570/ |