Nuclear Domains Involved in RNA Synthesis, RNA Processing, and Replication

Jong, Luitzen de; Grande, M.A.; Mattern, Karin; Schul, Wouter; Driel, Roel van

doi:10.1615/critreveukargeneexpr.v6.i2-3.60

Cited by 55 publications

(25 citation statements)

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“…Among the known NBs, POD or the PML bodies have been implicated in several cellular pathways, including the control of apoptosis (reviewed in reference 50), viral pathogenicity (reviewed in reference 49), and regulation of the higher-order chromatin structure (18). Nevertheless, in comparison to other well-studied NBs such as Cajal bodies or the speckles, it is still unclear whether PODs play an active role in nuclear events, i.e., whether they form as the result of nuclear events or are simply random accumulations of excess nuclear factors (45).…”

Section: Discussionmentioning

confidence: 99%

Sumoylation of p45/NF-E2: Nuclear Positioning and Transcriptional Activation of the Mammalian β-Like Globin Gene Locus

Shyu

Lee

Ting

et al. 2005

Molecular and Cellular Biology

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NF-E2 is a transcription activator for the regulation of a number of erythroid-and megakaryocytic lineagespecific genes. Here we present evidence that the large subunit of mammalian NF-E2, p45, is sumoylated in vivo in human erythroid K562 cells and in mouse fetal liver. By in vitro sumoylation reaction and DNA transfection experiments, we show that the sumoylation occurs at lysine 368 (K368) of human p45/NF-E2. Furthermore, p45 sumoylation enhances the transactivation capability of NF-E2, and this is accompanied by an increase of the NF-E2 DNA binding affinity. More interestingly, we have found that in K562 cells, the ␤-globin gene loci in the euchromatin regions are predominantly colocalized with the nuclear bodies promyelocytic leukemia protein (PML) oncogenic domains that are enriched with the PML, SUMO-1, RNA polymerase II, and sumoylatable p45/NF-E2. Chromatin immunoprecipitation assays further showed that the intact sumoylation site of p45/ NF-E2 is required for its binding to the DNase I-hypersensitive sites of the ␤-globin locus control region. Finally, we demonstrated by stable transfection assay that only the wild-type p45, but not its mutant form p45 (K368R), could efficiently rescue ␤-globin gene expression in the p45-null, erythroid cell line CB3. These data together point to a model of mammalian ␤-like globin gene activation by sumoylated p45/NF-E2 in erythroid cells.

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Section: Discussionmentioning

confidence: 99%

Sumoylation of p45/NF-E2: Nuclear Positioning and Transcriptional Activation of the Mammalian β-Like Globin Gene Locus

Shyu

Lee

Ting

et al. 2005

Molecular and Cellular Biology

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“…10I). The redistribution pattern may indicate that the precursor mRNA is associating with splicing factor-rich domains termed "nuclear speckles" (13). These nuclear splicing domains would process and ready the IFN-␥ mRNA for transport out of the nucleus.…”

Section: Il-12 Induces Nuclear Accumulation Of the Ifn-␥ Mrnamentioning

confidence: 99%

Regulation of Nuclear Gamma Interferon Gene Expression by Interleukin 12 (IL-12) and IL-2 Represents a Novel Form of Posttranscriptional Control

Hodge

Martı́nez

Julias

et al. 2002

Molecular and Cellular Biology

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Posttranscriptional control of gamma interferon (IFN-␥) gene expression has not been extensively studied and is poorly understood. Our work describes a posttranscriptional mechanism that modulates IFN-␥ mRNA expression in stimulated natural killer (NK) cells through nuclear retention of the IFN-␥ mRNA. This is evidenced by the elevated and sustained nuclear accumulation of both precursor and processed IFN-␥ mRNAs in NK cells stimulated with interleukin-12 (IL-12). The elevated nuclear mRNA accumulation persists long after transcriptional activity has subsided and the rate of cytoplasmic IFN-␥ mRNA accumulation has dropped. The IL-12-induced nuclear retention of the IFN-␥ mRNA prevails until a secondary cytokine stimulus is received. The secondary stimulus, which is initiated by IL-2, mediates transcription-independent movement of the nuclear IFN-␥ mRNA. Concurrent with the nucleocytoplasmic movement of the IFN-␥ mRNA, we have observed increases in the amount of processed nuclear IFN-␥ mRNA that are greater than that seen for the unprocessed IFN-␥ mRNA. The increase in processed IFN-␥ mRNA appears to be due to increased mRNA stability which then promotes increased nucleocytoplasmic shuttling of the mature IFN-␥ mRNA. These data support a model whereby mobilization of nuclear IFN-␥ mRNA stores allows NK cells to rapidly and robustly respond to secondary cytokine activators in a transcription-independent manner, thus shortening the time for overall cellular response to inflammatory signals.

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“…PML bodies have been implicated in many cellular pathways, including control of apoptosis (reviewed by Salomoni and Pandolfi, 2002;Eskiw and Bazett-Jones, 2002), viral pathogenicity (reviewed by Regard and Chelbi-Alix, 2001) and control of higher order chromatin structure (de Jong et al, 1996). Several models have been proposed for the function of PML bodies.…”

Section: Introductionmentioning

confidence: 99%

Size, position and dynamic behavior of PML nuclear bodies following cell stress as a paradigm for supramolecular trafficking and assembly

Eskiw

Dellaire

Mymryk

et al. 2003

Journal of Cell Science

122

137

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The promyelocytic leukemia (PML) protein has been implicated in many cellular pathways, but it is unclear whether the accumulation of PML and other proteins into PML nuclear bodies is a regulated or random process. In this paper we have used a variety of physiological stresses, including heat stress, Cd +2 exposure and adenovirus E1A expression, as tools to study the principles underlying the assembly/disassembly, integrity and dynamic behavior of PML bodies. Using live-cell imaging and immunofluorescence microscopy, we observe that PML bodies are positionally stable over time intervals of a few hours. After stress, however, microstructures form as a result of fission or budding from the surface of 'parental' PML bodies. Since new PML bodies do not form at new locations, and the relative sizes observed before heat shock are preserved after recovery, we conclude that there are pre-determined locations for PML bodies, and that they are not random accumulations of protein. Over-expression of small ubiquitin-like modifier (SUMO-1) prevents stressinduced disassembly of PML bodies, implicating SUMO-1 as a key regulator of PML body integrity. Stress-induced fission of SUMO-1-deficient microstructures from parental PML bodies may be a mechanism to change local chromatin domain environments by the dispersal of protein factors. PML bodies may provide a useful paradigm for the dynamics and integrity of other supramolecular protein complexes involved in processes such as transcription, RNA processing DNA repair and replication.Movies and supplemental data available online

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Nuclear Domains Involved in RNA Synthesis, RNA Processing, and Replication

Cited by 55 publications

References 0 publications

Sumoylation of p45/NF-E2: Nuclear Positioning and Transcriptional Activation of the Mammalian β-Like Globin Gene Locus

Sumoylation of p45/NF-E2: Nuclear Positioning and Transcriptional Activation of the Mammalian β-Like Globin Gene Locus

Regulation of Nuclear Gamma Interferon Gene Expression by Interleukin 12 (IL-12) and IL-2 Represents a Novel Form of Posttranscriptional Control

Size, position and dynamic behavior of PML nuclear bodies following cell stress as a paradigm for supramolecular trafficking and assembly

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