Histone acetylation is recruited in consolidation as a molecular feature of stronger memories
Gene expression is a key process for memory consolidation. Recently, the participation of epigenetic mechanisms like histone acetylation was evidenced in long-term memories. However, until now the training strength required and the persistence of the chromatin acetylation recruited are not well char...
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2009
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10720502_v16_n10_p600_Federman http://hdl.handle.net/20.500.12110/paper_10720502_v16_n10_p600_Federman |
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paper:paper_10720502_v16_n10_p600_Federman |
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paper:paper_10720502_v16_n10_p600_Federman2023-06-08T16:04:48Z Histone acetylation is recruited in consolidation as a molecular feature of stronger memories butyric acid histone histone H3 trichostatin A acetylation animal experiment animal tissue article biological model chromatin crab epigenetics gene expression regulation invertebrate long term memory male memory memory consolidation molecular interaction nonhuman parameter priority journal task performance training Western blotting Gene expression is a key process for memory consolidation. Recently, the participation of epigenetic mechanisms like histone acetylation was evidenced in long-term memories. However, until now the training strength required and the persistence of the chromatin acetylation recruited are not well characterized. Here we studied whether histone acetylation is involved in consolidation in invertebrates, whether it depends on the training strength, and whether it is a permanent or transient mechanism. We used a well-characterized memory model in invertebrates, the context-signal memory in crabs. Our results show no changes in histone 3 (H3) acetylation during consolidation of a standard training protocol. However, strong training induced a significant increase in H3 acetylation 1-h post-training, returning to basal levels afterward. Accordingly, the administration of histone deacetylase inhibitors sodium butyrate (NaB) and trichostatin A allowed a weak training to induce long-term memory. NaB enhanced memory in two phases during consolidation. These findings support that H3 acetylation (1) is involved in consolidation, (2) occurs only after strong training, (3) is a transient process, and (4) memory is enhanced in two phases. The coincidence of these phases with other mechanisms of gene expression is discussed. © 2009 Cold Spring Harbor Laboratory Press. 2009 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10720502_v16_n10_p600_Federman http://hdl.handle.net/20.500.12110/paper_10720502_v16_n10_p600_Federman |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
butyric acid histone histone H3 trichostatin A acetylation animal experiment animal tissue article biological model chromatin crab epigenetics gene expression regulation invertebrate long term memory male memory memory consolidation molecular interaction nonhuman parameter priority journal task performance training Western blotting |
| spellingShingle |
butyric acid histone histone H3 trichostatin A acetylation animal experiment animal tissue article biological model chromatin crab epigenetics gene expression regulation invertebrate long term memory male memory memory consolidation molecular interaction nonhuman parameter priority journal task performance training Western blotting Histone acetylation is recruited in consolidation as a molecular feature of stronger memories |
| topic_facet |
butyric acid histone histone H3 trichostatin A acetylation animal experiment animal tissue article biological model chromatin crab epigenetics gene expression regulation invertebrate long term memory male memory memory consolidation molecular interaction nonhuman parameter priority journal task performance training Western blotting |
| description |
Gene expression is a key process for memory consolidation. Recently, the participation of epigenetic mechanisms like histone acetylation was evidenced in long-term memories. However, until now the training strength required and the persistence of the chromatin acetylation recruited are not well characterized. Here we studied whether histone acetylation is involved in consolidation in invertebrates, whether it depends on the training strength, and whether it is a permanent or transient mechanism. We used a well-characterized memory model in invertebrates, the context-signal memory in crabs. Our results show no changes in histone 3 (H3) acetylation during consolidation of a standard training protocol. However, strong training induced a significant increase in H3 acetylation 1-h post-training, returning to basal levels afterward. Accordingly, the administration of histone deacetylase inhibitors sodium butyrate (NaB) and trichostatin A allowed a weak training to induce long-term memory. NaB enhanced memory in two phases during consolidation. These findings support that H3 acetylation (1) is involved in consolidation, (2) occurs only after strong training, (3) is a transient process, and (4) memory is enhanced in two phases. The coincidence of these phases with other mechanisms of gene expression is discussed. © 2009 Cold Spring Harbor Laboratory Press. |
| title |
Histone acetylation is recruited in consolidation as a molecular feature of stronger memories |
| title_short |
Histone acetylation is recruited in consolidation as a molecular feature of stronger memories |
| title_full |
Histone acetylation is recruited in consolidation as a molecular feature of stronger memories |
| title_fullStr |
Histone acetylation is recruited in consolidation as a molecular feature of stronger memories |
| title_full_unstemmed |
Histone acetylation is recruited in consolidation as a molecular feature of stronger memories |
| title_sort |
histone acetylation is recruited in consolidation as a molecular feature of stronger memories |
| publishDate |
2009 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10720502_v16_n10_p600_Federman http://hdl.handle.net/20.500.12110/paper_10720502_v16_n10_p600_Federman |
| _version_ |
1768544003834249216 |