Core filaments of the nuclear matrix.

He, Dacheng; Nickerson, Jeffrey A.; Penman, Sheldon

doi:10.1083/jcb.110.3.569

Cited by 424 publications

(388 citation statements)

References 41 publications

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“…The latter is a complex network of nuclear proteins and RNA (He et al, 1990;Pederson, 1998). We found that RNase treatment of permeabilized nuclei releases p53, as can be seen in Figure 1d.…”

Section: P53 In Hep G2 Cellssupporting

confidence: 58%

Non-activated p53 co-localizes with sites of transcription within both the nucleoplasm and the nucleolus

Rubbi

Milner

2000

Oncogene

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The p53 tumour suppressor functions as a sensor of genotoxic stress and, once activated, induces cell growth arrest or apoptosis. The precise intranuclear localization of latent p53 protein in non-stressed cells is unknown. Such information is essential in order to understand how relatively few molecules of p53 can detect and respond to DNA damage. Here we present the ®rst detailed supramolecular localization of p53 in the nuclei of cells under normal conditions of growth. We show that soluble, non-bound p53 is released by permeabilization, leaving structurally bound p53 in both the nucleus and nucleolus. In situ biochemical studies reveal (i) that nuclear-bound p53 is tethered by RNA (directly or indirectly) and (ii) that a sub-population of nuclearbound p53 co-localizes with sites of RNA synthesis. Transcriptional co-localization appeared to be independent of p53 conformation but dependent upon its quaternary structure. In the nucleolus p53 was observed at sites of rRNA synthesis and also adjacent to such sites. In contrast, nucleolar hdm-2 (shown by others to complex p53 and 5S RNA) was excluded from sites of rRNA synthesis. Our discovery that p53 is physically linked with sites of transcription may explain how relatively few p53 protein molecules can monitor genetic stress and respond preferentially to damage of actively transcribed genes. Oncogene (2000) 19, 85 ± 96.

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Section: P53 In Hep G2 Cellssupporting

confidence: 58%

Non-activated p53 co-localizes with sites of transcription within both the nucleoplasm and the nucleolus

Rubbi

Milner

2000

Oncogene

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“…This treatment further removes the components that are dependent on complex formation with RNA (16). Counterstaining of slides with DAPI (as described above) was used to monitor completeness of chromatin extraction.…”

Section: Methodsmentioning

confidence: 99%

High frequency of autoantibodies to insoluble cellular antigens in patients with chronic fatigue syndrome

Mikecz

Konstantinov

Buchwald

et al. 1997

Arthritis & Rheumatism

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Objective. To elucidate the humoral immune response in patients with chronic fatigue syndrome (CFS), by identification and characterization of autoantibodies.Methods. Initial immunofluorescence histochemistry studies of sera using human HEp-2 cell substrate were followed by antibody class subtyping and colocalization studies with reference antibodies. Association of CFS autoantigens with insoluble cellular components was determined by in situ extraction of soluble components and subsequent immunofluorescence histochemistry studies on the extracted cell substrate.Results. Of 60 CFS patients, 41 (68%) were positive for antinuclear antibodies. Localization of nuclear staining was found at the nuclear envelope (52%), in reticulated speckles (25%), in nucleoli (13%), and in dense fine speckles (5%). Twenty-eight CFS sera (47%) also had antibodies to cytoplasmic antigens. The major cytoplasmic staining pattern was of the intermediate filament type (35%). The observed nuclear envelope pattern of staining co-localized with lamina-associated polypeptide 2 (an integral nuclear membrane protein), the reticulated speckle pattern co-localized with nonsmall nuclear RNP splicing factor SC-35, and the Publication no. 9865MEM from The Scripps Research Institute.

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“…Fractionation of cellular proteins was performed as described 55 with some modifications. HCT116 cells were extracted in cytoskeleton buffer (CSK) (10 mM Pipes pH 6.8, 100 mM NaCl, 300 mM sucrose, 3 mM MgCl 2 , 1 mM EGTA, 0.5% Triton X-100) supplemented with 1 mM dithiothreitol, protease inhibitors (Complete; Roche Diagnostics) and phosphatase inhibitors (Cocktail I; Sigma).…”

Section: Cellular Fractionationmentioning

confidence: 99%

Hyperphosphorylation of RNA Polymerase II in Response to Topoisomerase I Cleavage Complexes and Its Association with Transcription- and BRCA1-dependent Degradation of Topoisomerase I

Sordet

Larochelle

Nicolas

et al. 2008

Journal of Molecular Biology

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SUMMARYThe progression of RNA polymerase II can be blocked by lesions on the DNA template. In this study, we focused in the modifications of the largest subunit of RNA polymerase II, Rpb1, in response to stabilized topoisomerase I (Top1)-DNA cleavage complexes. In addition to DNA modifications (base damages and strand breaks), Top1 cleavage complexes can be trapped by camptothecin and its derivatives used in cancer treatment. We find that, within a few minutes, camptothecin produces the complete hyperphosphorylation of Rpb1 in both primary and transformed cancer cells. Hyperphosphorylation is rapidly reversible following camptothecin removal. Hyperphosphorylation occurs selectively on the serine-5 residue of the conserved heptapeptide repeats in the Rpb1-carboxyterminal domain and is mediated principally by the TFIIH-associated kinase, Cdk7. Hyperphosphorylated Rpb1 is not primarily targeted for proteosomal degradation, but instead is subjected to cycles of phosphorylation and dephosphorylation as long as Top1 cleavage complexes are trapped by camptothecin. Finally, we show that transcription-induced degradation of Top1 is Brca1-dependent, suggesting a role for Brca1 in the repair or removal of transcription-blocking Top1-DNA cleavage complexes.

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Core filaments of the nuclear matrix.

Cited by 424 publications

References 41 publications

Non-activated p53 co-localizes with sites of transcription within both the nucleoplasm and the nucleolus

Non-activated p53 co-localizes with sites of transcription within both the nucleoplasm and the nucleolus

High frequency of autoantibodies to insoluble cellular antigens in patients with chronic fatigue syndrome

Hyperphosphorylation of RNA Polymerase II in Response to Topoisomerase I Cleavage Complexes and Its Association with Transcription- and BRCA1-dependent Degradation of Topoisomerase I

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