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      Mechanism of genome transcription in segmented dsRNA viruses

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          This chapter discusses the mechanism of genome transcription in segmented double-stranded RNA (dsRNA) viruses. Genome transcription is a critical stage in the life cycle of a virus, as this is the process by which the viral genetic information is presented to the host cell protein-synthesis machinery for the production of the viral proteins needed for genome replication and progeny virion assembly. Viruses with dsRNA genomes face a particular challenge in that host cells do not produce proteins that can transcribe from a dsRNA template. One of the more striking observations about genome transcription in dsRNA viruses is that this process occurs efficiently only when the transcriptionally competent particle is fully intact. This observation suggests that all of the components of the transcriptionally competent particle, including the viral genome, the transcription enzymes, and the viral capsid, function together to produce and release messenger RNA transcripts and that each component has a specific and critical role to play in promoting the efficiency of this process.

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          Identification of four conserved motifs among the RNA-dependent polymerase encoding elements.

          Four consensus sequences are conserved with the same linear arrangement in RNA-dependent DNA polymerases encoded by retroid elements and in RNA-dependent RNA polymerases encoded by plus-, minus- and double-strand RNA viruses. One of these motifs corresponds to the YGDD span previously described by Kamer and Argos (1984). These consensus sequences altogether lead to 4 strictly and 18 conservatively maintained amino acids embedded in a large domain of 120 to 210 amino acids. As judged from secondary structure predictions, each of the 4 motifs, which may cooperate to form a well-ordered domain, places one invariant amino acid in or proximal to turn structures that may be crucial for their correct positioning in a catalytic process. We suggest that this domain may constitute a prerequisite 'polymerase module' implicated in template seating and polymerase activity. At the evolutionary level, the sequence similarities, gap distribution and distances between each motif strongly suggest that the ancestral polymerase module was encoded by an individual genetic element which was most closely related to the plus-strand RNA viruses and the non-viral retroposons. This polymerase module gene may have subsequently propagated in the viral kingdom by distinct gene set recombination events leading to the wide viral variety observed today.
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            The atomic structure of the bluetongue virus core.

            The structure of the core particle of bluetongue virus has been determined by X-ray crystallography at a resolution approaching 3.5 A. This transcriptionally active compartment, 700 A in diameter, represents the largest molecular structure determined in such detail. The atomic structure indicates how approximately 1,000 protein components self-assemble, using both the classical mechanism of quasi-equivalent contacts, which are achieved through triangulation, and a different method, which we term geometrical quasi-equivalence.
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              Structure of the reovirus core at 3.6 A resolution.

              The reovirus core is an assembly with a relative molecular mass of 52 million that synthesizes, modifies and exports viral messenger RNA. Analysis of its structure by X-ray crystallography shows that there are alternative, specific and completely non-equivalent contacts made by several surfaces of two of its proteins; that the RNA capping and export apparatus is a hollow cylinder, which probably sequesters its substrate to ensure completion of the capping reactions; that the genomic double-stranded RNA is coiled into concentric layers within the particle; and that there is a protein shell that appears to be common to all groups of double-stranded RNA viruses.
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                Author and article information

                Journal
                Adv Virus Res
                Adv. Virus Res
                Advances in Virus Research
                Published by Elsevier Inc.
                0065-3527
                1557-8399
                7 January 2004
                2000
                7 January 2004
                : 55
                : 185-229
                Affiliations
                [a ]Verna and Moors McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine Houston, Texas 77030, USA
                [b ]Department of Molecular Virology and Microbiology, Baylor College of Medicine Houston, Texas 77030, USA
                Article
                S0065-3527(00)55004-0
                10.1016/S0065-3527(00)55004-0
                7131957
                11050943
                43d8aca9-dff0-4736-89d4-3e3ace1732f7
                Copyright © 2000 Published by Elsevier Inc.

                Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.

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