Mammalian nuclear speckles exhibit stable association with chromatin: a biochemical study
Nuclear Speckles (NS) are phase-separated condensates of protein and RNA whose components dynamically coordinate RNA transcription, splicing, transport and DNA repair. NS, probed largely by imaging studies, remained historically well known as Interchromatin Granule Clusters, and biochemical properti...
| Main Authors: | , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Taylor & Francis Group
2022-12-01
|
| Series: | Nucleus |
| Subjects: | |
| Online Access: | https://www.tandfonline.com/doi/10.1080/19491034.2021.2024948 |
| _version_ | 1818501303266967552 |
|---|---|
| author | Komal Raina Basuthkar J Rao |
| author_facet | Komal Raina Basuthkar J Rao |
| author_sort | Komal Raina |
| collection | DOAJ |
| description | Nuclear Speckles (NS) are phase-separated condensates of protein and RNA whose components dynamically coordinate RNA transcription, splicing, transport and DNA repair. NS, probed largely by imaging studies, remained historically well known as Interchromatin Granule Clusters, and biochemical properties, especially their association with Chromatin have been largely unexplored. In this study, we tested whether NS exhibit any stable association with chromatin and show that limited DNAse-1 nicking of chromatin leads to the collapse of NS into isotropic distribution or aggregates of constituent proteins without affecting other nuclear structures. Further biochemical probing revealed that NS proteins were tightly associated with chromatin, extractable only by high-salt treatment just like histone proteins. NS were also co-released with solubilised mono-dinucleosomal chromatin fraction following the MNase digestion of chromatin. We propose a model that NS-chromatin constitutes a “putative stable association” whose coupling might be subject to the combined regulation from both chromatin and NS changes.Abbreviations: NS: Nuclear speckles; DSB: double strand breaks; PTM: posttranslational modifications; DDR: DNA damage repair; RBP-RNA binding proteins; TAD: topologically associated domains; LCR: low complexity regions; IDR: intrinsically disordered regions. |
| first_indexed | 2024-12-10T20:54:19Z |
| format | Article |
| id | doaj.art-cb80136c89ce4263bf37131516f278c8 |
| institution | Directory Open Access Journal |
| issn | 1949-1034 1949-1042 |
| language | English |
| last_indexed | 2024-12-10T20:54:19Z |
| publishDate | 2022-12-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Nucleus |
| spelling | doaj.art-cb80136c89ce4263bf37131516f278c82022-12-22T01:34:00ZengTaylor & Francis GroupNucleus1949-10341949-10422022-12-01131587310.1080/19491034.2021.2024948Mammalian nuclear speckles exhibit stable association with chromatin: a biochemical studyKomal Raina0Basuthkar J Rao1Department of Biological Sciences, Tata Institute of Fundamental Research, Mumbai, IndiaDepartment of Biological Sciences, Tata Institute of Fundamental Research, Mumbai, IndiaNuclear Speckles (NS) are phase-separated condensates of protein and RNA whose components dynamically coordinate RNA transcription, splicing, transport and DNA repair. NS, probed largely by imaging studies, remained historically well known as Interchromatin Granule Clusters, and biochemical properties, especially their association with Chromatin have been largely unexplored. In this study, we tested whether NS exhibit any stable association with chromatin and show that limited DNAse-1 nicking of chromatin leads to the collapse of NS into isotropic distribution or aggregates of constituent proteins without affecting other nuclear structures. Further biochemical probing revealed that NS proteins were tightly associated with chromatin, extractable only by high-salt treatment just like histone proteins. NS were also co-released with solubilised mono-dinucleosomal chromatin fraction following the MNase digestion of chromatin. We propose a model that NS-chromatin constitutes a “putative stable association” whose coupling might be subject to the combined regulation from both chromatin and NS changes.Abbreviations: NS: Nuclear speckles; DSB: double strand breaks; PTM: posttranslational modifications; DDR: DNA damage repair; RBP-RNA binding proteins; TAD: topologically associated domains; LCR: low complexity regions; IDR: intrinsically disordered regions.https://www.tandfonline.com/doi/10.1080/19491034.2021.2024948Nuclear speckleschromatin-associationSR proteinsDNase 1speckle-associated chromatin |
| spellingShingle | Komal Raina Basuthkar J Rao Mammalian nuclear speckles exhibit stable association with chromatin: a biochemical study Nucleus Nuclear speckles chromatin-association SR proteins DNase 1 speckle-associated chromatin |
| title | Mammalian nuclear speckles exhibit stable association with chromatin: a biochemical study |
| title_full | Mammalian nuclear speckles exhibit stable association with chromatin: a biochemical study |
| title_fullStr | Mammalian nuclear speckles exhibit stable association with chromatin: a biochemical study |
| title_full_unstemmed | Mammalian nuclear speckles exhibit stable association with chromatin: a biochemical study |
| title_short | Mammalian nuclear speckles exhibit stable association with chromatin: a biochemical study |
| title_sort | mammalian nuclear speckles exhibit stable association with chromatin a biochemical study |
| topic | Nuclear speckles chromatin-association SR proteins DNase 1 speckle-associated chromatin |
| url | https://www.tandfonline.com/doi/10.1080/19491034.2021.2024948 |
| work_keys_str_mv | AT komalraina mammaliannuclearspecklesexhibitstableassociationwithchromatinabiochemicalstudy AT basuthkarjrao mammaliannuclearspecklesexhibitstableassociationwithchromatinabiochemicalstudy |