We are analyzing https://link.springer.com/article/10.1007/s10577-010-9161-8.

Title:
Dynamic as well as stable protein interactions contribute to genome function and maintenance | Chromosome Research
Description:
The cell nucleus is responsible for the storage, expression, propagation, and maintenance of the genetic material it contains. Highly organized macromolecular complexes are required for these processes to occur faithfully in an extremely crowded nuclear environment. In addition to chromosome territories, the nucleus is characterized by the presence of nuclear substructures, such as the nuclear envelope, the nucleolus, and other nuclear bodies. Other smaller structural entities assemble on chromatin in response to required functions including RNA transcription, DNA replication, and DNA repair. Experiments in living cells over the last decade have revealed that many DNA binding proteins have very short residence times on chromatin. These observations have led to a model in which the assembly of nuclear macromolecular complexes is based on the transient binding of their components. While indeed most nuclear proteins are highly dynamic, we found after an extensive survey of the FRAP literature that an important subset of nuclear proteins shows either very slow turnover or complete immobility. These examples provide compelling evidence for the establishment of stable protein complexes in the nucleus over significant fractions of the cell cycle. Stable interactions in the nucleus may, therefore, contribute to the maintenance of genome integrity. Based on our compilation of FRAP data, we propose an extension of the existing model for nuclear organization which now incorporates stable interactions. Our new “induced stability” model suggests that self-organization, self-assembly, and assisted assembly contribute to nuclear architecture and function.
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28 years and 1 months (reg. 1997-05-29).

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Keywords {🔍}

google, scholar, pubmed, nuclear, cas, cell, chromatin, assembly, protein, dna, biol, proteins, stable, bodies, cells, frap, selfassembly, nucleus, binding, components, pml, dynamic, replication, repair, transcription, complex, heterochromatin, fluorescence, residence, time, selforganization, dynamics, fig, esm, complexes, living, exchange, formation, interactions, sites, function, envelope, model, chromosome, sci, organization, vitro, molecules, mol, data,

Topics {✒️}

sumo-triggered rnf4/ubiquitin-mediated pathway live-cell imaging reveals damage-recognition protein xpc y-shaped multiprotein complex oligoheterocyclic pyridine-pyridazine strand nucleotide analog fluoro-uridine dna double-strand breaks actin-dependent intranuclear repositioning article download pdf e2f family members pml-interacting protein daxx full size image vitro single-molecule studies chromatin-binding protein complex tissue-derived primary cells double-layered nuclear membrane step-wise micelle association hyper-stable protein complexes key cell-cycle protein stable protein/chromatin complex gfp-tagged core histones homo-oligomerization properties assembles anti-telomere immunfluorescence data cell cycle-dependent manner home sweet home fluorescence fluctuation microscopy nuclear body-binding domains undergoes sumo-regulated polyubiquitylation competition–competent gal4 molecules pre-mrna splicing factors additional dna-binding proteins live cell imaging heterochromatin-binding protein ki-67 energy-driven motor activity plant cell-free system high-affinity binding sites h2a/h2b dimers combine single-particle tracking stable protein/chromatin complexes uv-induced lesions fluorescence correlation spectroscopy multiprotein complex cohesin nucleotide excision repair privacy choices/manage cookies fluorescent molecule concentration direct time-resolved observation helper molecule destabilize pml-nuclear body formation recent research dedicated term “assisted assembly”

Questions {❓}

Annunziato AT (2005) Split decision: what happens to nucleosomes during DNA replication?
Are the slowly recovering FRAPs for some nuclear components evidence for self-assembled nuclear structures?
Buscaino A, Allshire R, Pidoux A (2010) Building centromeres: home sweet home or a nomadic existence?
Constitutive heterochromatin: more stable than initially thought?
Matera AG, Izaguire-Sierra M, Praveen K, Rajendra TK (2009) Nuclear bodies: random aggregates of sticky proteins or crucibles of macromolecular assembly?
This model, of course, raises fundamental questions: When do helper molecules attach to their substrate during the cell cycle?
Von Mikecz A (2009) PolyQ fibrillation in the cell nucleus: who’s bad?

Schema {🗺️}

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         description:The cell nucleus is responsible for the storage, expression, propagation, and maintenance of the genetic material it contains. Highly organized macromolecular complexes are required for these processes to occur faithfully in an extremely crowded nuclear environment. In addition to chromosome territories, the nucleus is characterized by the presence of nuclear substructures, such as the nuclear envelope, the nucleolus, and other nuclear bodies. Other smaller structural entities assemble on chromatin in response to required functions including RNA transcription, DNA replication, and DNA repair. Experiments in living cells over the last decade have revealed that many DNA binding proteins have very short residence times on chromatin. These observations have led to a model in which the assembly of nuclear macromolecular complexes is based on the transient binding of their components. While indeed most nuclear proteins are highly dynamic, we found after an extensive survey of the FRAP literature that an important subset of nuclear proteins shows either very slow turnover or complete immobility. These examples provide compelling evidence for the establishment of stable protein complexes in the nucleus over significant fractions of the cell cycle. Stable interactions in the nucleus may, therefore, contribute to the maintenance of genome integrity. Based on our compilation of FRAP data, we propose an extension of the existing model for nuclear organization which now incorporates stable interactions. Our new “induced stability” model suggests that self-organization, self-assembly, and assisted assembly contribute to nuclear architecture and function.
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            Human Genetics
            Animal Genetics and Genomics
            Plant Genetics and Genomics
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      headline:Dynamic as well as stable protein interactions contribute to genome function and maintenance
      description:The cell nucleus is responsible for the storage, expression, propagation, and maintenance of the genetic material it contains. Highly organized macromolecular complexes are required for these processes to occur faithfully in an extremely crowded nuclear environment. In addition to chromosome territories, the nucleus is characterized by the presence of nuclear substructures, such as the nuclear envelope, the nucleolus, and other nuclear bodies. Other smaller structural entities assemble on chromatin in response to required functions including RNA transcription, DNA replication, and DNA repair. Experiments in living cells over the last decade have revealed that many DNA binding proteins have very short residence times on chromatin. These observations have led to a model in which the assembly of nuclear macromolecular complexes is based on the transient binding of their components. While indeed most nuclear proteins are highly dynamic, we found after an extensive survey of the FRAP literature that an important subset of nuclear proteins shows either very slow turnover or complete immobility. These examples provide compelling evidence for the establishment of stable protein complexes in the nucleus over significant fractions of the cell cycle. Stable interactions in the nucleus may, therefore, contribute to the maintenance of genome integrity. Based on our compilation of FRAP data, we propose an extension of the existing model for nuclear organization which now incorporates stable interactions. Our new “induced stability” model suggests that self-organization, self-assembly, and assisted assembly contribute to nuclear architecture and function.
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      dateModified:2010-11-03T00:00:00Z
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         Fluorescence microscopy
         FRAP
         Multi-protein complex
         Chromatin binding
         Dynamics
         Residence time
         Induced stability
         Assisted assembly
         Self-assembly
         Self-organization
         Cell Biology
         Human Genetics
         Animal Genetics and Genomics
         Plant Genetics and Genomics
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      affiliation:
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               type:PostalAddress
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