Results 301 to 310 of about 768,924 (317)
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Picornavirus RNA-dependent RNA polymerase
The International Journal of Biochemistry & Cell Biology, 2009Replication of the picornavirus genome is catalysed by a viral encoded RNA-dependent RNA polymerase, termed 3D polymerase. Together with other viral and host proteins, this enzyme performs its functions in the cytoplasm of host cells. The crystal structure of 3D polymerase from a number of picornaviruses has been determined.
Peter C. McMinn, Chee Choy Kok
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2004
At the end of the 1950s Hoagland and Zamecnik had succeeded in obtaining an in vitro protein synthesis from ribosomes and crude acellular extracts. Ribosomes cannot by themselves achieve a specific protein synthesis and require an information originating in last analysis in the genes.
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At the end of the 1950s Hoagland and Zamecnik had succeeded in obtaining an in vitro protein synthesis from ribosomes and crude acellular extracts. Ribosomes cannot by themselves achieve a specific protein synthesis and require an information originating in last analysis in the genes.
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Ribosomal RNA Synthesis and RNA Polymerase
Nature, 1970MULTIPLE forms of RNA polymerase activity have been isolated from developing sea-urchin embryos, rat liver nuclei and calf thymus1–3. The molecular basis of this heterogeneity is at present unknown but, whatever its basis, the crucial question seems to be whether different enzymes copy different genes.
G. P. Tocchini-Valentini, M. Crippa
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Critical Reviews in Biochemistry, 1985
This review will attempt to cover the present information on the multiple forms of eukaryotic DNA-dependent RNA polymerases, both at the structural and functional level. Nuclear RNA polymerases constitute a group of three large multimeric enzymes, each with a different and complex subunit structure and distinct specificity.
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This review will attempt to cover the present information on the multiple forms of eukaryotic DNA-dependent RNA polymerases, both at the structural and functional level. Nuclear RNA polymerases constitute a group of three large multimeric enzymes, each with a different and complex subunit structure and distinct specificity.
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[9] Reconstitution of RNA polymerase
1996Publisher Summary The DNA-dependent RNA polymerase of Escherichia coli is composed of core enzyme and one of at least six molecular species of the σ subunit. Despite the complexity of its subunit composition and its extraordinarily large molecular size, RNA polymerase is one of the few large molecular assemblies that can be successfully ...
Nobuyuki Fujita, Akira Ishihama
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RNA-dependent RNA polymerases in RNA silencing
Biological Chemistry, 2011Abstract RNA-dependent RNA polymerases (RdRPs) synthesize double-stranded RNAs that are processed into small RNAs and mediate gene silencing. Viral RdRPs and cellular RdRPs show little structural homology to each other. Cellular RdRPs play key roles in RNA silencing by producing complementary strands for target RNAs via Dicer-dependent and -
Yoshiko Maida, Kenkichi Masutomi
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1973
Publisher Summary This chapter presents the status of RNA polymerases involved in RNA synthesis in mammalian cells, with emphasis on some recent developments in the field of nuclear RNA polymerase. The chapter discusses that the RNA polymerases of eukaryotic nuclei exist in multiple forms. These enzymes are compartmentalized within the nucleus.
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Publisher Summary This chapter presents the status of RNA polymerases involved in RNA synthesis in mammalian cells, with emphasis on some recent developments in the field of nuclear RNA polymerase. The chapter discusses that the RNA polymerases of eukaryotic nuclei exist in multiple forms. These enzymes are compartmentalized within the nucleus.
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Inhibition of RNA polymerase by RNA
Journal of Molecular Biology, 1963Suzanne Bourgeois +2 more
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RNA Polymerase and the Control of RNA Synthesis
1969Publisher Summary This chapter discusses the mechanism of RNA polymerase action in terms of the regulation of RNA synthesis. The evidence presented indicates that accurate and selective transcription of DNA can be achieved with very pure RNA polymerase.
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