Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.27.5 (RNase)
 17,967 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The interaction of protein and RNA in composition of virion ribonucleoprotein (RNP) of influenza A virus was studied by treatment of this structure with hydrolytic enzymes: pancreatic RNase A, nuclease S1 and pronase. The results indicate that RNA in RNP does not shield proteins from the effect of pronase. The possibility of using this fact in the construction of a model RNP structure is discussed. No differences in the effect of RNase A and nuclease S1 on RNP were found which corresponded to the concept of the protective role of RNP protein in the process of RNA hydrolysis.
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PMID:[Action of hydrolytic enzymes on influenza virus A ribonucleoprotein]. 627 94

The sequence of 2,191 nucleotides encoding the env gene of murine retrovirus Akv was determined by using a molecular clone of the Akv provirus. Deduction of the encoded amino acid sequence showed that a single open reading frame encodes a 638-amino acid precursor to gp70 and p15E. In addition, there is a typical leader sequence preceding the amino terminus of gp70. The locations of potential glycosylation sites and other structural features indicate that the entire gp70 molecule and most of p15E are located on the outer side of the membrane. Internal cleavage of the env precursor to generate gp70 and p15E occurs immediately adjacent to several basic amino acids at the carboxyl terminus of gp70. This cleavage generates a region of 42 uncharged, relatively hydrophobic amino acids at the amino terminus of p15E, which is located in a position analogous to the hydrophobic membrane fusion sequence of influenza virus hemagglutinin. The mature polypeptides are predicted to associate with the membrane via a region of 30 uncharged, mostly hydrophobic amino acids located near the carboxyl terminus of p15E. Distal to this membrane association region is a sequence of 35 amino acids at the carboxyl terminus of the env precursor, which is predicted to be located on the inner side of the membrane. By analogy to Moloney murine leukemia virus, a proteolytic cleavage in this region removes the terminal 19 amino acids, thus generating the carboxyl terminus of p15E. This leaves 15 amino acids at the carboxyl terminus of p15E on the inner side of the membrane in a position to interact with virion cores during budding. The precise location and order of the large RNase T(1)-resistant oligonucleotides in the env region were determined and compared with those from several leukemogenic viruses of AKR origin. This permitted a determination of how the differences in the leukemogenic viruses affect the primary structure of the env gene products.
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PMID:Nucleotide sequence of the Akv env gene. 628 70

The addition of detergent-solubilized influenza C virus to a reaction mixture containing ATP, CTP, GTP, [3H]UTP, and Mg2+ leads to the synthesis of an acid-insoluble, radioactive product, which is ribonuclease-sensitive. The dinucleoside monophosphate ApG clearly enhances the reaction rate, a fact which indicates that influenza C viruses follow the same strategy of transcription as influenza A and B viruses, the other members of the orthomyxovirus family.
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PMID:Influenza-C-virion-associated RNA-dependent RNA-polymerase activity. 654 51

The hemagglutinin (HA) gene of the influenza virus subtype H1N1 isolated from pigs and birds has been analyzed by the hybridization technique. According to the RNase protection data the HA genes of recent isolates from pigs in Northern Europe are genetically more closely related to those of isolates from birds in Europe and North America than to those of isolates from pigs in the United States, Taiwan, and Italy. Thus, two different H1N1 subtypes are circulating in the pig population. The results are consistent with the view that H1N1 viruses can be transmitted from birds to pigs and/or vice versa.
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PMID:Genetic relatedness of hemagglutinins of the H1 subtype of influenza A viruses isolated from swine and birds. 662 31

Ribonucleoprotein (RNP) cores with RNA-synthesizing activity were prepared in two fractions, M protein-free and M protein-associated, from detergent-treated influenza virus PR8 by centrifugation through a discontinuous triple gradient of cesium sulfate, glycerol, and NP-40. The M-free RNP was fractionated by phosphocellulose column chromatography into two major RNP forms, A and B, which differed in the content of P proteins, while the M-associated RNP gave only the low P-content Form-B RNP. Starting from the high P-content Form-A RNP, an RNA-P proteins complex virtually free from NP protein was isolated by cesium sulfate equilibrium centrifugation. The complex, containing only three P proteins (P1, P2, and P3), was still active in catalyzing RNA synthesis in vitro without addition of exogenous template, indicating that NP protein is not required for the catalysis of RNA synthesis. RNA synthesis by the isolated RNA-P proteins complex was dependent on either ApG or capped RNA primers, and required four ribonucleoside triphosphates as substrates. The RNA product in this reaction was hybridizable to viral RNA. A complex of one each of the three P proteins was separated from RNA by glycerol gradient centrifugation after ribonuclease treatment or cesium chloride equilibrium centrifugation.
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PMID:RNA polymerase of influenza virus. III. Isolation of RNA polymerase-RNA complexes from influenza virus PR8. 686 42

RNA and protein interaction in the structure of influenza virus ribonucleoprotein (RNP) was studied by ultraviolet (UV) irradiation. After UV-irradiation of virion RNP for 1 hour only 6% of 3H-uridine-labeled RNA was found to go into the aqueous phase upon phenol-detergent extraction. Pretreatment of RNP with small doses of pancreatic RNase before RNA extraction slightly increased (up to 18%) the amount of RNA going into the aqueous phase. About 90% RNA was found after extraction in the aqueous phase in the nonirradiated material. As a result of UV-irradiation of RNP, RNA in RNP became more resistant to RNase: the residual acid-insoluble radioactivity was 21% whereas with nonirradiated RNP it was 3.2%. The results of the analysis of RNP labeled for protein in polyacrylamide gel and SDS-sucrose gradient after UV-irradiation and ribonuclease treatment indicate the formation of UV-induced linkages between RNA and NP protein.
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PMID:[RNA-protein interactions in influenza virus A ribonucleoprotein detected by UV radiation]. 733 92

Influenza virus nucleoid ("core") was obtained by the treatment of virions with hydrolytic enzymes without the use of fixing agents. The "core" buoyant density in sucrose density gradient was 1.24 g/cm3. The subvirus particles are completely devoid of surface proteins, glycoproteins, and their polypeptide composition is represented by group P proteins; NP and M proteins. RNA in the core is insensitive to the effect of RNase. Morphological analysis by electron microscopy revealed the presence of spherical compact particles without spikes on their surface.
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PMID:[Preparation and investigation of some properties of influenza virus nucleoid]. 738 86

A ribonuclease activity associated with influenza virus has been purified to homogeneity. This preparation is free of DNAase, phosphodiesterase, and phosphatase activities. The purified enzyme has a pH optima of 7.0 at 37 degrees C, and moves as a single band on sodium dodecyl sulfate - polyacrylamide gel with an estimated molecular weight of 84 000.
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PMID:The isolation and properties of a ribonuclease associated with influenza virus. 738 74

By molecular hybridization and by neuraminidase inhibition tests it is shown that all influenza A strains tested carrying an Nav3 or Nav2 neuraminidase (NA) are genetically highly related in their NA genes and cross-react serologically with specific antineuraminidase sera. The Nav6 strains exhibit a very low RNase protection after hybridization and do not cross-react serologically with Nav2 or Nav3 strains. Thus, the Nav2 and Nav3 strains comprise one group which is distinct from that of Nav6 strains.
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PMID:Genetic relatedness of the neuramindase of influenza A strains Nav2, Nav3, and Nav6. 741 73

The genetic and antigenic variability of the G glycoproteins from 76 human respiratory syncytial (RS) viruses (subgroup A) isolated during six consecutive epidemics in either Montevideo, Uruguay, or Madrid, Spain, have been analyzed. Genetic diversity was evaluated for all viruses by the RNase A mismatch cleavage method and for selected strains by dideoxy sequencing. The sequences reported here were added to those published for six isolates from Birmingham, United Kingdom, and for two reference strains (A2 and Long), to derive a phylogenetic tree of subgroup A viruses that contained two main branches and several subbranches. During the same epidemic, viruses from different branches were isolated. In addition, closely related viruses were isolated in distant places and in different years. These results illustrate the capacity of the virus to spread worldwide, influencing its mode of evolution. The antigenic analysis of all isolates was carried out with a panel of anti-G monoclonal antibodies that recognized strain-specific (or variable) epitopes. A close correlation between genetic relatedness and antigenic relatedness in the G protein was observed. These results, together with an accumulation of amino acid changes in a major antigenic area of the G glycoprotein, suggest that immune selection may be a factor influencing the generation of RS virus diversity. The pattern of RS virus evolution is thus similar to that described for influenza type B viruses, expect that the level of genetic divergence among the G glycoproteins of RS virus isolates is the highest reported for an RNA virus gene product.
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PMID:Evolutionary pattern of human respiratory syncytial virus (subgroup A): cocirculating lineages and correlation of genetic and antigenic changes in the G glycoprotein. 805 27


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