Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: UMLS:C0038362 (stomatitis)
8,852 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In vitro transcriptase activity of three group I temperature-sensitive (ts) mutants of vesicular stomatitis virus restricted at 39 C was restored by L-protein fractions derived from wild-type (wt) vesicular stomatitis virion nucleo-capsids. Soluble NS protein from wt nucleocapsids did not reconstitute restricted transcriptions of the group I RNA-ts mutants. NS protein activity, but not L protein activity, was purified from the group I ts mutants; this NS fraction always displayed the wt phenotype in reconstitution assays. Neither the L nor the NS protein was capable of restoring the defective transcriptive activity of the group IV vesicular stomatitis virus mutant ts W16B.
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PMID:RNA- temperature-sensitive mutants of vesicular stomatitis virus: L-protein thermosensitivity accounts for transcriptase restriction of group I mutants. 17

The RNA-dependent RNA polymerase associated with vesicular stomatitis virus was isolated to apparent homogeneity by a newly developed procedure, which includes stepwise removal of proteins from virions by successive treatment with high concentrations of cesium sulfate and cesium chloride, followed by glycerol gradient centrifugation or chromatography on phosphocellulose or DEAE-Sephadex column. The polymerase thus purified contained L (large protein) and NS proteins as the intrinsic subunits and multiple species of enzyme were found which differ in the molar ratio of L to NS. Since the enzyme with the highest activity was composed of equimolar amounts of the two subunits and exhibited the sedimentation coefficient of approximately 11 S in a buffer containing 0.2 M NaCl, the structure of active protomer was suggested to be (L)1(NS)1. In accordance with this conclusion, enzyme preparations deficient in the content of NS protein, were activated by the addition of preparations deficient in the content of NS protein. The purified RNA polymerase catalyzed the synthesis of poly(A), which was covalently attached to the 3' termini of RNA products, and RNA, only in the presence of all 4 substrates. The present finding might be the first which indicates that the transcriptase itself catalyzes post-transcriptional modification of mRNA by adding poly(A) sequences to the 3'-OH termini. The molecular mechanism of the switch from transcription to poly(A) synthesis, however, remains to be investigated.
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PMID:Function and structure of RNA polymerase from vesicular stomatitis virus. 18 23

The intracellular transcriptase complex of vesicular stomatitis virus-infected L cells synthesized RNA complementary to the entire infectious virus genome at either 37 degrees C or 28 degrees C in vitro. Not all sequences were present at the same frequency, however; copies of that segment of the genome common to the LT defective particles were present at 20 to 100 times higher frequently than copies of the genome segment common to the ST defective particle. The less frequent region was transcribed somewhat more effectively at 28 degrees C than at 37 degrees C. The results suggest that transcriptional regulation rather than selective degradation is responsible for the differential accumulation of RNA.
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PMID:Analysis of in vitro transcription products of intracellular vesicular stomatitis virus RNA polymerase. 18 12

The RNA polymerase in cells infected with three group I mutants of vesicular stomatitis virus has been examined. Mouse L cells were incubated at the permissive temperature (30 degrees C) for a few hours after infection to allow the development of secondary transcription. The temperature dependence of the secondary transcription system was determined from the incorporation of labelled uridine, in the presence of cycloheximide, at 30 and at 38 degrees C, the later temperature being non-permissive for viral replication. In cells infected with mutants W14, W28, and G11 at a low multiplicity (20 PFU/cells) secondary transcriptase activity was markedly temperature-sensitive after 3 and 5 h of infection at 30 degrees C. At a high multiplicity of infection (1000 PFU/cell) cells infected with W28 showed considerable RNA synthesis at 38 degrees C after 3 h at 30 degrees C. RNA synthesis was also observed in W28-infected cells in which protein synthesis was allowed to continue after the shift from 30 to 38 degrees C. In the latter two cases the RNA synthesized contained 12-18S species but little or no 30S mRNA.
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PMID:Temperature-sensitive mutants of vesicular stomatitis virus: viral RNA synthesis in cells infected with mutants belonging to complementation group I. 18 5

The ability of certain vesicular stomatitis virus (VSV; Indiana serotype) temperature-sensitive (ts) mutants to synthesize intracellular viral complementary RNA (vcRNA) at permissive or nonpermissive temperatures for productive infections has been investigated. Mutants belonging to complementation groups II, III, and V synthesize RNA at nonpermissive temperature in amounts essentially equivalent to that obtained at permissive temperatures. Mutant ts G I-114 possesses a thermolabile transcriptase and does not synthesize vcRNA at 40 degrees C; however, mutants ts O I-5, O I-53, O I-78, and O I-80 possess thermostabile transcriptases that are capable of some vcRNA synthesis at 40 degrees C. All five group I mutants are defective in their secondary transcription ability at 40 degrees C. Wild-type VSV New Jersey virus is able to complement the transcription defect of ts G I-114 at 40 degrees C. This complementation is inhibited by puromycin, suggesting that a viral gene product of VSV New Jersey (e.g., its transcriptase or a transcriptase component) is involved. Mokola virus is not able to complement the ts G I-114 defect, although Mokola does synthesize vcRNA in infected cells (in the presence or absence of cycloheximide).
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PMID:Synthesis of RNA by mutants of vesicular stomatitis virus (Indiana serotype) and the ability of wild-type VSV New Jersey to complement the VSV Indiana ts G I-114 transcription defect. 18 10

An in vitro transcription system in which vesicular stomatitis virus (VSV) mRNA species have been synthesized is described. In addition to purified VSV virions, which contain an RNA-dependent RNA polymerase, this system contained a cytoplasmic cell extract that enhanced correct transcription. Gel electrophoretic analysis of the methylated polyadenylic acid [poly(A)]-containing VSV mRNA produced in this system in the presenct of S-adenosylmethionine showed the discrete VSV mRNA species. However, when unmethylated mRNA was synthesized in the presence of S-adenosylhomocysteine, the poly(A)-containing transcripts were large and heterogeneous in molecular weight and did not contain discrete VSV mRNA species. Two-dimensional fingerprint analysis of the methylated and unmethylated products suggested that identical nucleotide sequences were present in the RNAs. Further analysis showed the presence of very large heterogeneous poly(A), 200 to 2,000 nucleotides in lenght, in the unmethylated transcript. Proof that this large poly(A) was covalently linked to the correct VSV mRNA transcripts was obtained by removal of the poly(A) by hybirdization with oligodeoxythymidylic acid and digestion with RNase H. This digestion produced unmethylated VSV mRNA transcripts with the same discrete sizes as the deadenylated RNAs produced from VSV mRNA initially isolated from VSV-infected cells. The results suggest that there is a relationship between methylation at the 5'-end and polyadenylation at the 3'-end of VSV mRNA's. Furthermore, addition of the very large poly(A) does not affect the normal process of sequential transcription of the VSV genome, suggesting that this poly(A) addition is occurring independently of further transcription.
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PMID:Giant heterogeneous polyadenylic acid on vesicular stomatitis virus mRNA synthesized in vitro in the presence of S-adenosylhomocysteine. 18 93

We established previously that the temperature-dependent host range mutant, td CE 3, of vesicular stomatitis virus (VSV) New Jersey possesses temperature-sensitive RNA transcriptase activity. In this paper, we describe dissociation and reconstitution experiments designed to determine which VSV polypeptide is affected by the td CE 3 mutation. Wild-type VSV New Jersey (ts+), the temperature-dependent host range mutant (td CE 3), and the revertant of this mutant (td CE/R1) were used. Transcribing nucleoprotein preparations, isolated from purified virus particles, were treated in the presence of digitonin with either 0.9 M LiCl to produce supernatants containing virtually only the L polypeptide or 2.0 M LiCl to produce ribonucleoprotein pellets containing only the polypeptides N and NS. Supernatant and pellet fractions synthesized either no or only trace amounts of RNA in vitro. Reconstitution of the supernatants with the pellets in all combinations at 31 degrees C restored much of the transcriptase activity of the transcribing nucleoprotein preparations. RNA synthesis occurred at 39 degrees C when the three pellets were reconstituted with wild-type and revertant supernatants. However, supernatant of the mutant td CE 3 reconstituted with any of the three pellets resulted in little or no detectable transcriptase activity at 39 degrees C. This implies that the polypeptide affected by the td CE 3 mutation is the L polypeptide.
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PMID:Temperature-dependent host range mutation in vesicular stomatitis virus affecting polypeptide L. 19 60

In addition to an RNA-dependent RNA polymerase, purified vesicular stomatitis virus contains a methyltransferase activity which transfers the methyl group from the methyl donor, S-adenosyl-L-methionine, to two positions in the 5'-terminal capped structure of the nascent mRNA's synthesized in vitro as 7mG-(5)'ppp(5')Apm... In the present study it is shown that two distinct methyltransferase activities are discernible in the purified virus. The in vitro concentrations of the methyl donor specify the number and location of the methyl groups transferred to the capped 5'-termini of VSV mRNA's. Limited concentrations of the methyl donor result in a single methylation of the penultimate base in the 2'-hydroxyl position, that is, G(5')ppp(5')Apm..., whereas saturating concentrations of the methyl donor methylate the blocking guanosine residue at the 7-position, resulting in the dimethylated cap, 7mG(5')ppp(5')Apm... Pulse-chase experiments demonstrate that the monomethylated cap structure is the precursor substrate for the dimethylated cap. In this respect, vesicular stomatitis virus system is quite distinct from the vaccinia and reovirus systems. Virus purified from different host cells including hamster, mouse, and human contain both methyltransferase activities. The mRNA's containing monomethylated capped structures are poor templates for protein synthesis in vitro.
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PMID:Two methyltransferase activities in the purified virions of vesicular stomatitis virus. 20 77

The RNA-dependent RNA polymerase associated with vesicular stomatitis virus has been found to be markedly inhibited at high concentrations of virus. This endogenous inhibitor of the virion transcriptase was completely reversed by the action of two negatively charged polyamino acids: poly(L-glutamic acid) and pepsin (EC 3.4.23.1). Two other polyanions, heparin and polyethylene sulfonate, strongly inhibited the activity of the virion transcriptase even at low virus concentrations. Poly (L-glutamic acid) rapidly released the block in transcription of concentrated vesicular stomatitis virus, possibly owing to competition for binding sites of the inhibitor on the virion nucleocapsid transcription complex.
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PMID:Reversal by certain polyanions of an endogenous inhibitor of the vesicular stomatitis virus-associated transcriptase. 20 38

The L and NS proteins of vesicular stomatitis virions (New Jersey serotype) were solubilized with Triton X-100 and high-salt buffer and recombined with purified nucleocapsids under conditions similar to those used to reconstitute transcriptase activity in vitro. The nucleocapsid-bound L and NS proteins were separated from unbound proteins on a glycerol gradient. The rebinding of L and NS proteins mimics the in vivo binding in that at saturation the ratio of L and NS molecules to N molecules is approximately the same as observed in the intact virion. L and NS proteins were separated and added back independently and in combination to the template. The purified NS protein bound to the template in the absence of L protein. However, the L protein binding appeared to depend on the presence of NS protein. The presence of Mg2+ and nucleotides, which is required for transcription, was not necessary for the rebinding of L and NS proteins.
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PMID:Rebinding of transcriptase components (L and NS proteins) to the nucleocapsid template of vesicular stomatitis virus. 21 81


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