Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder
Abstract The nucleolus is essential for ribosome biogenesis and is involved in many other cellular functions. We performed a systematic spatiotemporal dissection of the human nucleolar proteome using confocal microscopy. In total, 1,318 nucleolar proteins were identified; 287 were localized to fibri...
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| Format: | Article |
| Language: | English |
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Springer Nature
2020-08-01
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| Series: | Molecular Systems Biology |
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| Online Access: | https://doi.org/10.15252/msb.20209469 |
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| author | Lovisa Stenström Diana Mahdessian Christian Gnann Anthony J Cesnik Wei Ouyang Manuel D Leonetti Mathias Uhlén Sara Cuylen‐Haering Peter J Thul Emma Lundberg |
| author_facet | Lovisa Stenström Diana Mahdessian Christian Gnann Anthony J Cesnik Wei Ouyang Manuel D Leonetti Mathias Uhlén Sara Cuylen‐Haering Peter J Thul Emma Lundberg |
| author_sort | Lovisa Stenström |
| collection | DOAJ |
| description | Abstract The nucleolus is essential for ribosome biogenesis and is involved in many other cellular functions. We performed a systematic spatiotemporal dissection of the human nucleolar proteome using confocal microscopy. In total, 1,318 nucleolar proteins were identified; 287 were localized to fibrillar components, and 157 were enriched along the nucleoplasmic border, indicating a potential fourth nucleolar subcompartment: the nucleoli rim. We found 65 nucleolar proteins (36 uncharacterized) to relocate to the chromosomal periphery during mitosis. Interestingly, we observed temporal partitioning into two recruitment phenotypes: early (prometaphase) and late (after metaphase), suggesting phase‐specific functions. We further show that the expression of MKI67 is critical for this temporal partitioning. We provide the first proteome‐wide analysis of intrinsic protein disorder for the human nucleolus and show that nucleolar proteins in general, and mitotic chromosome proteins in particular, have significantly higher intrinsic disorder level compared to cytosolic proteins. In summary, this study provides a comprehensive and essential resource of spatiotemporal expression data for the nucleolar proteome as part of the Human Protein Atlas. |
| format | Article |
| id | doaj-art-cbf6f48dc6aa4e2ab84c21448c6a9ce1 |
| institution | Kabale University |
| issn | 1744-4292 |
| language | English |
| publishDate | 2020-08-01 |
| publisher | Springer Nature |
| record_format | Article |
| series | Molecular Systems Biology |
| spelling | doaj-art-cbf6f48dc6aa4e2ab84c21448c6a9ce12025-08-20T03:46:41ZengSpringer NatureMolecular Systems Biology1744-42922020-08-0116811610.15252/msb.20209469Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorderLovisa Stenström0Diana Mahdessian1Christian Gnann2Anthony J Cesnik3Wei Ouyang4Manuel D Leonetti5Mathias Uhlén6Sara Cuylen‐Haering7Peter J Thul8Emma Lundberg9Science for Life Laboratory, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of TechnologyScience for Life Laboratory, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of TechnologyScience for Life Laboratory, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of TechnologyChan Zuckerberg BiohubScience for Life Laboratory, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of TechnologyChan Zuckerberg BiohubScience for Life Laboratory, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of TechnologyCell Biology and Biophysics Unit, European Molecular Biology LaboratoryScience for Life Laboratory, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of TechnologyScience for Life Laboratory, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of TechnologyAbstract The nucleolus is essential for ribosome biogenesis and is involved in many other cellular functions. We performed a systematic spatiotemporal dissection of the human nucleolar proteome using confocal microscopy. In total, 1,318 nucleolar proteins were identified; 287 were localized to fibrillar components, and 157 were enriched along the nucleoplasmic border, indicating a potential fourth nucleolar subcompartment: the nucleoli rim. We found 65 nucleolar proteins (36 uncharacterized) to relocate to the chromosomal periphery during mitosis. Interestingly, we observed temporal partitioning into two recruitment phenotypes: early (prometaphase) and late (after metaphase), suggesting phase‐specific functions. We further show that the expression of MKI67 is critical for this temporal partitioning. We provide the first proteome‐wide analysis of intrinsic protein disorder for the human nucleolus and show that nucleolar proteins in general, and mitotic chromosome proteins in particular, have significantly higher intrinsic disorder level compared to cytosolic proteins. In summary, this study provides a comprehensive and essential resource of spatiotemporal expression data for the nucleolar proteome as part of the Human Protein Atlas.https://doi.org/10.15252/msb.20209469human protein atlasintrinsic protein disordernucleolusperichromosomal layer |
| spellingShingle | Lovisa Stenström Diana Mahdessian Christian Gnann Anthony J Cesnik Wei Ouyang Manuel D Leonetti Mathias Uhlén Sara Cuylen‐Haering Peter J Thul Emma Lundberg Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder Molecular Systems Biology human protein atlas intrinsic protein disorder nucleolus perichromosomal layer |
| title | Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder |
| title_full | Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder |
| title_fullStr | Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder |
| title_full_unstemmed | Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder |
| title_short | Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder |
| title_sort | mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder |
| topic | human protein atlas intrinsic protein disorder nucleolus perichromosomal layer |
| url | https://doi.org/10.15252/msb.20209469 |
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