Topic
Nucleolar chromatin
About: Nucleolar chromatin is a research topic. Over the lifetime, 170 publications have been published within this topic receiving 6776 citations.
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TL;DR: Escherichia coliRNA polymerase and the endogenous engaged RNA polymerase I were used as specific probes to monitor the physiologically inactive and active nucleolar chromatin template function, respectively.
17 citations
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TL;DR: It is shown that preribosomal components as monitored by a ribosomal protein leave the nucleolus, while a large proportion of RNA polymerase I remains associated with the nucleolar chromatin, i.e. probably the pre-rRNA genes, during inactivation of transcription.
17 citations
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TL;DR: Using a protocol centered on affinity chromatography, the purification of the androgen receptor protein to a state approaching homogeneity has been accomplished, and the purified receptor stimulates the RNA polymerase A and protein kinase activities associated with prostate nucleolar chromatin.
17 citations
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TL;DR: The use of nucleolar silver staining in plant cells in conditions of impaired transcription, either natural (quiescent cells) or induced (actinomycin D, ethidium bromide and cordycepin treatments), shows that nucleoli with very low transcription rates, compared with controls, contain similar amounts of argyrophilic proteins, as well as the same structural location.
17 citations
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TL;DR: It is proposed that host factor‐mediated viral chromatin remodeling and concomitant ViPR body formation are prerequisites for efficient encapsidation of Ad chromatin.
Abstract: The adenovirus (Ad) genome is believed to be packaged into the virion by forming a chromatin-like structure. The replicated viral genome is likely to be condensed through binding with viral core proteins before encapsidation. Replicated viral genomes accumulate in the central region of the nucleus, which we termed virus-induced postreplication (ViPR) body. However, the molecular mechanism by which the nuclear structure is reorganized and its functional significance in virus production are currently not understood. In this study, we found that viral packaging protein IVa2, but not capsid proteins, accumulated in the ViPR body. In addition, nucleolar chromatin regulatory proteins, nucleophosmin 1 (NPM1), upstream binding factor, and nucleolin accumulated in the ViPR body in late-stage Ad infection. NPM1 depletion increased the nuclease-resistant viral genome and delayed the ViPR body formation. These results suggested that structural changes in the infected cell nucleus depend on the formation of viral chromatin by host chromatin regulatory proteins. Because NPM1 depletion decreases production of the infectious virion, we propose that host factor-mediated viral chromatin remodeling and concomitant ViPR body formation are prerequisites for efficient encapsidation of Ad chromatin.
15 citations