Yellows
Mostrando 25-36 de 61 artigos, teses e dissertações.
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25. Organization of beet yellows-virus inclusions in leaf cells of beta.
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26. CHANGES IN THE COMPOSITION OF THE TOMATO PLANT ACCOMPANYING DIFFERENT STAGES OF YELLOWS 12
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27. Mycoplasma-like bodies in the salivary glands of insect vectors carrying the aster yellows agent.
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28. P0 of Beet Western Yellows Virus Is a Suppressor of Posttranscriptional Gene Silencing
Higher plants employ a homology-dependent RNA-degradation system known as posttranscriptional gene silencing (PTGS) as a defense against virus infection. Several plant viruses are known to encode proteins that can suppress PTGS. Here we show that P0 of beet western yellows virus (BWYV) displays strong silencing suppressor activity in a transient expression a
American Society for Microbiology.
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29. Phylogeny of mycoplasmalike organisms (phytoplasmas): a basis for their classification.
A global phylogenetic analysis using parsimony of 16S rRNA gene sequences from 46 mollicutes, 19 mycoplasmalike organisms (MLOs) (new trivial name, phytoplasmas), and several related bacteria placed the MLOs definitively among the members of the class Mollicutes and revealed that MLOs form a large discrete monophyletic clade, paraphyletic to the Acholeplasma
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30. Coat protein gene duplication in a filamentous RNA virus of plants.
Computer-assisted analysis revealed a striking sequence similarity between the putative 24-kDa protein (p24) encoded by open reading frame (ORF) 5 of beet yellows closterovirus and the coat protein of this virus encoded by the adjacent ORF6. Both of these proteins are closely related to the homologous proteins of another closterovirus, citrus tristeza virus.
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31. Enzymatic activities in cell fractions of mycoplasmalike organisms purified from aster yellows-infected plants.
Mycoplasmalike organisms (MLOs), purified from aster yellows-infected plants were osmotically lysed, and the membranes were separated from the cytoplasmic fraction through differential centrifugation. Electron microscopic examinations of sections of the purified MLOs and the isolated membranes showed pleomorphic bodies and unit membranous empty vesicles, res
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32. Complex molecular architecture of beet yellows virus particles
Closteroviruses possess exceptionally long filamentous virus particles that mediate protection and active transport of the genomic RNA within infected plants. These virions are composed of a long “body” and short “tail” whose principal components are the major and minor capsid proteins, respectively. Here we use biochemical, genetic, and ultrastructu
National Academy of Sciences.
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33. Phytoplasma-specific PCR primers based on sequences of the 16S-23S rRNA spacer region.
In order to develop a diagnostic tool to identify phytoplasmas and classify them according to their phylogenetic group, we took advantage of the sequence diversity of the 16S-23S intergenic spacer regions (SRs) of phytoplasmas. Ten PCR primers were developed from the SR sequences and were shown to amplify in a group-specific fashion. For some groups of phyto
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34. Sequence heterogeneity in the two 16S rRNA genes of Phormium yellow leaf phytoplasma.
Phormium yellow leaf (PYL) phytoplasma causes a lethal disease of the monocotyledon, New Zealand flax (Phormium tenax). The 16S rRNA genes of PYL phytoplasma were amplified from infected flax by PCR and cloned, and the nucleotide sequences were determined. DNA sequencing and Southern hybridization analysis of genomic DNA indicated the presence of two copies
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35. The 64-Kilodalton Capsid Protein Homolog of Beet Yellows Virus Is Required for Assembly of Virion Tails
The filamentous virion of the closterovirus Beet yellows virus (BYV) consists of a long body formed by the major capsid protein (CP) and a short tail composed of the minor capsid protein (CPm) and the virus-encoded Hsp70 homolog. By using nano-liquid chromatography-tandem mass spectrometry and biochemical analyses, we show here that the BYV 64-kDa protein (p
American Society for Microbiology.
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36. Leader Proteinase of Beet Yellows Virus Functions in Long-Distance Transport
The 66-kDa leader proteinase (L-Pro) of the Beet yellows virus (BYV) possesses a nonconserved N-terminal domain and a conserved, papain-like C-terminal domain. Previous work revealed that the N-terminal domain functions in RNA amplification, whereas the C-terminal domain is required for autoproteolysis. Alanine-scanning mutagenesis was applied to complete th
American Society for Microbiology.