RNA polymerase II is aberrantly phosphorylated and localized to viral replication compartments following herpes simplex virus infection

Rice, Stephen A.; Long, Melissa C.; Lam, Vivian; Spencer, Charlotte A.

doi:10.1128/jvi.68.2.988-1001.1994

Cited by 142 publications

(105 citation statements)

References 99 publications

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“…3 b). This absence of staining is in sharp contrast to the pronounced replication compartment staining seen for other host cell DNA-binding proteins such as RNAP II, basal transcription factors, p53, Rb, and DNA ligase, as well as for viral replication and regulatory proteins such as ICP4, ICP8, ICP27, and viral replication proteins (Wilcock and Lane 1991; Rice et al 1994; Zhong and Hayward 1997; de Bruyn Kops et al 1998). These data suggest that histones H3 and H4 do not contribute significantly to the protein complement of HSV nucleoprotein fibers.…”

Section: Resultsmentioning

confidence: 61%

“…Herpes simplex virus type 1 (HSV-1) is a >150-kD nuclear DNA virus whose genome is transcribed by host RNAP II (Smiley et al 1991). Within 3–4 h postinfection, RNAP II and host transcription factors are recruited from the host genome onto the viral genome, and become concentrated in subnuclear foci known as viral replication compartments which are sites of viral DNA replication and transcription (de Bruyn Kops and Knipe 1988; Rice et al 1994; Phelan et al 1997). BrdU is rapidly incorporated into viral replication compartments and viral DNA remains within replication compartments after its synthesis (de Bruyn Kops and Knipe 1988; Phelan et al 1997).…”

Section: Resultsmentioning

confidence: 99%

“…HSV replication compartments are also sites of viral and cellular regulatory protein accumulation. In keeping with their role in viral gene transcription, these structures recruit host RNA polymerase II, TBP and basal transcription factors, as well as the viral transcription activator protein ICP4 (Randall and Dinwoodie 1986; Knipe et al 1987; Rice et al 1994; de Bruyn Kops et al 1998; Spencer, C., unpublished data). ICP4 is a sequence-specific and nonspecific DNA-binding protein, and DNA binding is essential for its gene activation function (Kattar-Cooley and Wilcox 1989; Michael and Roizman 1989; Allen and Everett 1997).…”

Section: Resultsmentioning

confidence: 99%

“…As virus infection proceeds, host transcription is repressed and viral gene transcription is activated in a controlled temporal order (Godowski and Knipe 1986; Rice et al 1994; Spencer et al 1997). Because viral and host cell genes contain similar RNAP II promoter elements and use the same transcription machinery, this global change in transcription may be due, in part, to nucleotide sequence-independent mechanisms, such as differences between host and viral chromatin structure (Smiley et al 1991).…”

Section: Resultsmentioning

confidence: 99%

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Mitotic Transcription Repression in Vivo in the Absence of Nucleosomal Chromatin Condensation

Spencer

Kruhlak

Jenkins

et al. 2000

The Journal of Cell Biology

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All nuclear RNA synthesis is repressed during the mitotic phase of the cell cycle. In addition, RNA polymerase II (RNAP II), nascent RNA and many transcription factors disengage from DNA during mitosis. It has been proposed that mitotic transcription repression and disengagement of factors are due to either mitotic chromatin condensation or biochemical modifications to the transcription machinery. In this study, we investigate the requirement for chromatin condensation in establishing mitotic transcription repression and factor loss, by analyzing transcription and RNAP II localization in mitotic cells infected with herpes simplex virus type 1. We find that virus-infected cells enter mitosis and that mitotic viral DNA is maintained in a nucleosome-free and noncondensed state. Our data show that RNAP II transcription is repressed on cellular genes that are condensed into mitotic chromosomes and on viral genes that remain nucleosome free and noncondensed. Although RNAP II may interact indirectly with viral DNA during mitosis, it remains transcriptionally unengaged. This study demonstrates that mitotic repression of transcription and loss of transcription factors from mitotic DNA can occur independently of nucleosomal chromatin condensation.

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Section: Resultsmentioning

confidence: 61%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

Mitotic Transcription Repression in Vivo in the Absence of Nucleosomal Chromatin Condensation

Spencer

Kruhlak

Jenkins

et al. 2000

The Journal of Cell Biology

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“…Indeed, both in vitro and in somatic cells, transcription involves a cycle of phosphorylation/dephosphorylation of the carboxy-terminal domain (CTD) of this subunit (reviewed in Emili and Ingles, 1995;Dahmus, 1996). Moreover, phosphorylation of the CTD is altered in response to stimuli which have a general influence on the transcriptional activity of the cells, such as viral infection (Rangel et al, 1987;Rice et al, 1994), growth-factor release from quiescence (Dubois et al, 1994b), heat-shock (Venetianer et al, 1995) and meiotic maturation (Bellier et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Nuclear translocation and carboxyl-terminal domain phosphorylation of RNA polymerase II delineate the two phases of zygotic gene activation in mammalian embryos

Bellier

Chastant-Maillard

Adenot³

et al. 1997

The EMBO Journal

102

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In mammalian embryos, zygotic gene transcription initiates after a limited number of cell divisions through a two-step process termed the zygotic gene activation (ZGA). Here we report that RNA polymerase II undergoes major changes in mouse and rabbit preimplantation embryos during the ZGA. In transcriptionally inactive unfertilized oocytes, the RNA polymerase II largest subunit is predominantly hyperphosphorylated on its carboxy-terminal domain (CTD). The CTD is markedly dephosphorylated several hours after fertilization, before the onset of a period characterized by a weak transcriptional activity. The largest subunit of RNA polymerase II then lacks immunological and drug-sensitivity characteristics related to its phosphorylation by the TFIIH-associated kinase and gradually translocates into the nuclei independently of DNA replication and mitosis. A phosphorylation pattern of the largest subunit, close to that observed in somatic cells, is established in both mouse and rabbit embryos at the stage when transcription becomes a requirement for further development (respectively at the 2-and 8/16-cell stage). As these events occurred in the presence of actinomycin D, the nuclear translocation of RNA polymerase II and the phosphorylation of the CTD might be major determinants of ZGA.

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Functional Domains within the Nucleus of a Cell Infected with HSV-1

Phelan

Clements

1997

Rev. Med. Virol.

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HSV‐1 is a nuclear replicating DNA virus capable of establishing both lytic and latent infections in mammalian cells. Expression of the more than 80 HSV genes (the majority of which do not contain introns) requires complex coordination of viral and cellular factors both temporally, at appropriate points during the infectious cycle, and spatially as the virus transcription, replication and DNA packaging factories develop in the cell nucleus. Whilst the HSV genome encodes sufficient proteins to sustain viral DNA replication, it is reliant upon its host cell for RNA polymerase II and RNA processing machinery, in addition to an increasing number of cellular cofactors, for gene expression. As HSV establishes a lytic infection, cellular gene expression and splicing are inhibited as cellular chromatin is displaced and a dramatic reorganisation of the host cell nucleus occurs. The formation of large protein‐rich factories synthesising viral RNA and replicating and packaging the viral genomes is the most striking alteration. In addition to the synthetic factories, large clumps of cellular and viral intron‐containing RNAs accumulate in the nucleus as a result of the inhibition of splicing, at locations which colocalise with splicing factors, but are separate from transcription sites. An essential HSV protein IE63, discussed here, has been identified with a role in the organisation of the nucleus at many levels including replication and transcription site formation, splicing factor organisation and the transport of RNA. This review is a summary of our present understanding of the organisation of the HSV infected cell nucleus, relating viral genomes, RNA, DNA and proteins in the context of the nucleus. However this is a rapidly evolving field and new factors (both viral and cellular) involved in the regulation of these functional domains are constantly being identified. © 1997 by John Wiley & Sons, Ltd.

show abstract

RNA polymerase II is aberrantly phosphorylated and localized to viral replication compartments following herpes simplex virus infection

Cited by 142 publications

References 99 publications

Mitotic Transcription Repression in Vivo in the Absence of Nucleosomal Chromatin Condensation

Mitotic Transcription Repression in Vivo in the Absence of Nucleosomal Chromatin Condensation

Nuclear translocation and carboxyl-terminal domain phosphorylation of RNA polymerase II delineate the two phases of zygotic gene activation in mammalian embryos

Functional Domains within the Nucleus of a Cell Infected with HSV-1

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