Partial characterization of the structural proteins of sonchus yellow net virus

Jackson, A.O.

doi:10.1016/0042-6822(78)90169-1

Cited by 35 publications

(34 citation statements)

References 32 publications

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“…SYNV encodes six genes in a negative-sense orientation; these six genes encode a nucleocapsid protein (N), a phosphoprotein (P), a putative movement protein (sc4), a matrix protein (M), a glycoprotein (G), and a large polymerase protein (L). The N, P, and L proteins are components of an infectious nucleocapsid core (15) with RNA-dependent RNA polymerase activity that can be purified from the nuclei of virus-infected cells (34,35). These core components form viroplasm-like structures within the nucleus that are thought to be the sites of viral replication (22).…”

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Role of the Sonchus Yellow Net Virus N Protein in Formation of Nuclear Viroplasms

Deng

Bragg²,

Ruzin³

et al. 2007

J Virol

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Plant rhabdoviruses are classified into the genera Cytorhabdovirus and Nucleorhabdovirus on the basis of their sites of replication, morphogenesis, and maturation (for a review, see reference 17). Sonchus yellow net nucleorhabdovirus (SYNV) replicates in the nucleus and is the most extensively characterized among the plant rhabdoviruses. SYNV encodes six genes in a negative-sense orientation; these six genes encode a nucleocapsid protein (N), a phosphoprotein (P), a putative movement protein (sc4), a matrix protein (M), a glycoprotein (G), and a large polymerase protein (L). The N, P, and L proteins are components of an infectious nucleocapsid core (15) with RNA-dependent RNA polymerase activity that can be purified from the nuclei of virus-infected cells (34,35). These core components form viroplasm-like structures within the nucleus that are thought to be the sites of viral replication (22). The N protein contains a carboxy (C)-terminal bipartite nuclear localization signal (NLS) that is required for nuclear import (7). The P protein when expressed alone localizes both inside and outside of the nucleus, but coexpression of the N and P proteins in plant and yeast (Saccharomyces cerevisiae) cells results in formation of compact subnuclear foci that are reminiscent of viroplasms (7). Sedimentation and immunological analyses have shown that in vivo associations of the N, P, and L proteins are required for RNA-dependent RNA polymerase activity (35). Yeast two-hybrid analyses and affinity chromatography experiments have also verified homologous (N-N) and heterologous (N-P) binding that is mediated by a region near the amino (N) terminus of the N protein (7). These results indicate that complex interactions of the N, P, and L proteins are required for subnuclear viroplasm formation and that the nucleocapsid cores within the viroplasms function in replication of genomic and antigenomic RNAs and in mRNA transcription (17).In the current study, we have conducted experiments to define the contributions of the N protein to the formation of viroplasms. These experiments include refined mapping to identify amino acids in an N-terminal helix-loop-helix motif of the N protein that result in subnuclear localization and N-N and N-P protein binding. We have also shown that mutations within the helix-loop-helix motif that disrupt N-N and N-P interactions interfere with the formation of subnuclear foci. The C-terminal NLS that is required for nuclear import of the N protein (7) mediates binding to importin ␣ homologues from yeast (ySrp1) and plant Arabidopsis thaliana (AtSrp1), but the P protein fails to bind to the importin ␣ homologues. These

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Role of the Sonchus Yellow Net Virus N Protein in Formation of Nuclear Viroplasms

Deng

Bragg²,

Ruzin³

et al. 2007

J Virol

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“…We have previously identified five discrete SYNV-complementary (sc) RNAs, or viral-encoded mRNAs, that were designated scRNAs 1-5 and have postulated that these mRNAs encode the five structural proteins L, G, N, Ml, and M2, respectively (5). The putative locations of these proteins within the virion and their electrophoretic patterns (9) are consistent with the nomenclature proposed for rhabdoviruses (10), but the genome organization and sequences at the junctions of all of the genes have not previously been determined.…”

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Physical map of the genome of sonchus yellow net virus, a plant rhabdovirus with six genes and conserved gene junction sequences.

Heaton

Hillman

Hunter

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

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We provide evidence that a plant rhabdovirus, sonchus yellow net virus (SYNV), is similar to most animal rhabdoviruses in the order of structural genes and in the nucleotide sequences at the gene junctions but that it differs in the presence and location of a putative nonstructural gene. From the patterns of hybridization of a library of recombinant DNA clones, we have shown that the SYNV genome is transcribed into a short 3'-terminal "leader RNA" and six mRNAs. The proteins encoded by the SYNV mRNAs, in order of the appearance of their genes in the SYNV genome, are designated 3'-N-

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“…This is indeed the case (Table 1). The molecular weights of the G and N proteins (77000 and 64000; Jackson & Christie, 1977;Jackson, 1978) are close to the maximum coding capacities of vc2 and vc3. Although the molecular weight of the L protein has not been unequivocally determined, the L proteins of other plant and animal rhabdoviruses range in molecular weight from 150000 to 170000 (Peters, 1981).…”

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“…These proteins are believed to be associated with the viral envelope (Jackson, 1978;Morrison, 1979). The total complexity of these vcRNA species is in agreement with previous estimates of 40 to 50 ~ of the genome, based on hybridization in solution .…”

Section: Short Communicationmentioning

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Characterization of Viral-complementary RNA Associated with Polyribosomes from Tobacco Infected with Sonchus Yellow Net Virus

Milner

Jackson

1983

Journal of General Virology

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SUMMARYPolyribosomal RNA from tobacco infected with sonchus yellow net virus was resolved by electrophoresis on agarose gels, transferred to nitrocellulose and hybridized to radioactive viral RNA. Polyadenylated RNA contained four major viral complementary species, molecular weights 2.2 x 106, 0.83 x 106, 0.62 x 106 and 0.46 × 106, plus a minor species, molecular weight approx. 3 × 106. No such species could be detected in the non-polyadenylated RNA fraction. The polyadenylated RNA from membrane-bound polyribosomes contained only the 0-83 × 106 and 0-46 x 106 molecular weight RNAs. The sizes of the RNAs were consistent with the expected sizes of messages for the virus proteins, calculated from the molecular weight of these proteins.

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Partial characterization of the structural proteins of sonchus yellow net virus

Cited by 35 publications

References 32 publications

Role of the Sonchus Yellow Net Virus N Protein in Formation of Nuclear Viroplasms

Role of the Sonchus Yellow Net Virus N Protein in Formation of Nuclear Viroplasms

Physical map of the genome of sonchus yellow net virus, a plant rhabdovirus with six genes and conserved gene junction sequences.

Characterization of Viral-complementary RNA Associated with Polyribosomes from Tobacco Infected with Sonchus Yellow Net Virus

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