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Query: EC:3.1.27.3 (RNase T1)
 1,228 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

RNA oligonucleotide fingerprint analyses indicate that the genome RNA obtained from Trinidad donkey (TRD) Venezuelan equine encephalomyelitis (VEE) virus serotype I A, its vaccine strain derivative TC-83, and the VEE I B virus isolate PTF-39, have almost identical patterns of characteristic ribonuclease T1 resistant oligonucleotides. The TC-83 strain and the I B isolate can, on the basis of these analyses, be considered as variants of the TRD virus and categorized as I AB serotypes. Comparisons made by single and co-electrophoreses of the ribonuclease T1 digests of the RNA species of TC-83 and a VEE I C isolate P676 indicate that 16 of 37 large oligonucleotides of the TC-83 virus co-migrate with the oligonucleotides obtained from the I C isolate. Similar single and co-electrophoreses of ribonuclease T1 digests of the RNA species of TC-83 and a VEE I D isolate 3880 indicate that 18 of 41 TC-83 large oligonucleotides co-migrate with the oligonucleotides obtained from the I D virus isolate. At least nine of the TC-83 large oligonucleotides appear on the basis of these analyses, to be present in the digests of the genome RNA obtained from these selected I B, I C and I D virus isolates. The ribonucleast T1 digests of three I E virus isolates (Mina II, 63U2 and 71U388) give oligonucleotide fingerprints which, although comparable to each other, are more distinct from the I A and I B RNA fingerprints than are those of the I C and I D RNA species. The ribonuclease T1 resistant oligonucleotide fingerprints of VEE virus isolates belonging to serotypes (VEE subtypes) II, III and IV show little similarity to each other or to those of the serotype I virus isolates we have studied. The results obtained here agree with the reported close antigenic relationships of VEE, I A, I B, I C and I D virus isolates, and our studies suggest that these viruses have conserved nucleotide sequences. The I E virus isolates appear to have more distinct nucleotide sequences than do the other serotype 1 viruses. The results also agree with the serological differentiation of VEE, I, II, III and IV subtypes in that the oligonucleotide fingerprints of subtypes II to IV are different from each other and from those of the different serotype I virus isolates. On the basis of antigenic and genome relationships, VEE isolates can be classified as serotypes I to IV with serotype I viruses differentiated into the categories I AB, I C, I D and I E.
J Gen Virol 1979 May
PMID:Immunochemical and oligonucleotide fingerprint analyses of Venezuelan equine encephalomyelitis complex viruses. 9 Jan 15

A comparison has been made of some of the biochemical and serological characteristics of five isolates of foot-and-mouth disease virus (FMDV), serotype A. Three of the viruses have been assigned to the same subtype, A22; the other two belong to different subtypes, A5 and A24. RNA competition hybridization and two-dimensional electrophoresis of the oligonucleotides produced by ribonuclease T1 showed that the three A22 viruses formed a group which could be distinguished from the A5 and A24 viruses. However, the three A22 viruses showed some differences by both tests. Analysis of the virus polypeptides by polyacrylamide gel electrophoresis methods also distinguished the A22 viruses as a group distinct from the A5 and A24 viruses, but small differences within the A22 group were observed using electrofocusing techniques. Serological differences were observed between the viruses using complement fixation tests and by competition radioimmunoassay with antisera obtained from guinea pigs infected with these viruses. The greatest similarity occurred between the viruses previously subtyped as A22, with A5 and A24 being distinct from the A22 group and from each other. The relationship of the biochemical and serological data is discussed.
J Gen Virol 1979 Dec
PMID:Comparative biochemical and serological analysis of five isolates of a single serotype of foot-and-mouth disease virus. 9 48

Fragments of foot-and-mouth disease virus RNA of decreasing size, containing the 3' poly(A) sequence have been prepared by alkali treatment and sucrose gradient centrifugation followed by oligo(dT)-cellulose affinity chromatography. Polyacrylamide gel electrophoresis of the ribonuclease T1 resistant oligonucleotides from these polyadenylated fragments has enabled us to locate the position of some of the longer oligonucleotides on the RNA. In particular the poly C tract has been shown to be near the 5' end of the RNA; The possible function of the poly(C) tract is discussed in the light of these findings.
J Gen Virol 1976 Dec
PMID:The location of the ploy(C) tract in the RNA of foot-and-mouth disease virus. 18 24

A comparison has been made of some of the serological and physicochemical properties of a virulent and an avirulent strain of foot-and-mouth disease virus, serotype SAT1. The avirulent strain (SAT1-82) was derived from the virulent strain (SAT1-7) by serial passage in BHK 21 cells. The viruses were indistinguishable in cross-neutralization tests. In immunodiffusion tests a clear spur line was obtained with the SAT1-82 antiserum but not with SAT1-7 antiserum. The major polypeptides of the two viruses were identical when examined by polyacrylamide gel electrophoresis. Hybridization and thermal denaturation experiments failed to distinguish between the RNAs but two-dimensional electrophoresis of the oligonucleotides produced by ribonuclease T1 digestion revealed several differences. Possibly the most significant of these differences was the size of the polycytidylic acid [poly (C)] tract. There were about 170 nucleotides in the poly (C) tract of the SAT1-7 RNA compared with around 100 in the SAT1-82 RNA. Further evidence for this deletion was provided by the slightly different behaviour of the two RNAs when compared by sucrose gradient centrifugation and polyacrylamide gel electrophoresis.
J Gen Virol 1977 Jan
PMID:Biochemical analysis of a virulent and an avirulent strain of foot-and-mouth disease virus. 18 83

The abilities of purine- and pyrimidine-requiring mutants to produce six orthophosphate repressible extracellular enzymes, alkaline phosphatase, 5'-nucleotidase, acid phosphatase, two nucleases and ribonuclease N1 were examined by culturing these mutants in low and high phosphate media containing nucleotide or nucleoside. All the purine requiring mutants produced significantly reduced amounts of alkaline phosphatase, 5'-nucleotidase, acid phosphatase, alkaline nuclease and acid nuclease ranging 0.5-4.2, 5.0-17.4, 25.0-100, 20.3-67.5 and 6.2-48.5%, respectively. Production of ribonuclease N1 was found to be rather stimulated (150-564%) in these mutants. Essentially the same results were obtained for pyrimidine requiring mutants. Among those mutants ad-2 and ad-9 showed relatively high enzyme producing activity. Especially the production of ribonuclease N1 in ad-2 and ad-9 ranged to 4.9- and 5.6-fold that in the wild type. Though nuc-1 mutant (A1) has no ability to produce all these six repressible enzymes, double mutants A1ad-2 and A1ad-9 produced a significant amount of ribonuclease N1 in low and high phosphate media and acid phosphatase in low phosphate media.
Mol Gen Genet 1977 Feb 28
PMID:Control of the Production of orthophosphate repressible extracellular enzymes in Neurospora crassa. 19 39

Techniques are described for the growth and rapid purification of the avian coronavirus infectious bronchitis virus (IBV). Purified IBV has a sedimentation coefficient of 320S and a buoyant density of 1.22 g/ml in sucrose-deuterium oxide equilibrium gradients. IBV RNA extracted by proteinase K in the presence of sodium dodecyl sulfate and further purified by phenol extraction and gradient centrifugation is single stranded and has a sedimentation coefficient of 64S, as determined by isokinetic gradient centrifugation. Analysis on sucrose gradients under both aqueous and denaturing conditions together with agarose gel electrophoresis in the presence of the chaotropic agent methylmercuric hydroxide gave a value of 8 X 10(6) for the moleclar weight of IBV RNA. This value was confirmed by RNase T1 fingerprinting, which also indicated that IBV RNA is haploid. No evidence was found of subunit structure in IBV RNA. From these results together with the recently reported observation that IBV RNA is infectious and contains a tract of polyadenylic acid (Lomniczi, J. Gen. Virol., in press), we conclude that the genome of the coronaviruses is a single continuous chain of about 23,000 mononucleotides that is of messenger polarity.
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PMID:Genome of infectious bronchitis virus. 19 90

The 32P-labelled genomes of poliovirus type 1, 2 and 3 have been digested with RNase T1 and the products separated by two-dimensional gel electrophoresis. All three fingerprints differ in the separation pattern of the large oligonucleotides. The molar yields of the large RNase T1-resistant oligonucleotides of type 1 and type 2 RNA of poliovirus RNA are close to one. By comparing the yields of these oligonucleotides to the amount of RNA from which they originated, the chain length of type 1 poliovirus RNA was found to be 7851 +/- 567 nucleotides (mol. wt. 2.66 +/- 0.19 x 10(6) and that of poliovirus type 2, 8181 +/- 578 nucleotides (mol. wt. 2.77 +/- 0.19 x 10(6). The chain length of two defective interfering particle (DI) RNAs of poliovirus type 1 were determined to be 7042 +/- 999 nucleotides for DI(1) and 6639 +/- 674 nucleotides for DI(2).
J Gen Virol 1979 Aug
PMID:Sequence studies of poliovirus RNA. IV. Nucleotide sequence complexities of poliovirus type 1, type 2 and two type 1 defective interfering particles RNAs, and fingerprint of the poliovirus type 3 genome. 23 Feb 85

The RNA-dependent RNA polymerase induced in BHK 21 cells by infection with foot-and-mouth disease virus has been isolated from the replication complex. It contains a major, virus-coded protein with mol. wt. 56 000 which appears from serological studies and tryptic peptide mapping to be the same as the virus infection associated (VIA) antigen and the protein P56 found in cells infected with the virus. Other virus coded proteins and a host cell protein were present in the partially purified replication complex but were removed by digestion with ribonuclease T1, leaving only the major virus coded protein. The tryptic peptide maps of the VIA antigen of the seven serotypes of the virus were similar, suggesting a high level of conservation in that region of the genome coding for the RNA polymerase of each type.
J Gen Virol 1979 Nov
PMID:Purification and identification of the RNA-dependent RNA polymerase of foot-and-mouth disease virus. 23 34

Transcription of Escherichia coli ribosomal DNA introduced into Proteus mirabilis on F14 is described. We have developed an assay for E. coli coded ribosomal RNA involving fingerprinting of ribonuclease T1 digests of RNA isolated from ribosomal subunits. Sequence differences in the ribosomal RNA of the two species have allowed us to detect E. coli coded 16S, 23S, and 5S ribosomal RNA in ribosomal subunits of the E. coli-P. mirabilis hybrid. The proportion of E. coli coded rRNA in the hybrid is found at a level which is compatible with the number of E. coli (and P. mirabilis) ribosomal DNA sequences. The resulting ribosomal RNA appears in ribosomes in a form which indicates extensive compatibility of E. coli coded ribosomal RNA with P. mirabilis ribosomal proteins and maturational factors.
Mol Gen Genet 1976 Aug 19
PMID:Transcription of Escherichia coli ribosomal DNA in Proteus mirabilis. 78 56

Destabilizing events required for subsequent cotranslational disassembly of tobacco mosaic virus (TMV) particles in vitro were studied. Brief treatment of U-32P-labelled TMV (strain vulgare or U2) with 1% SDS exposed only 2.5% of the RNA (160 5' nucleotides) in a susceptible subpopulation of virions. Limited uncoating occurred almost immediately and appeared to be synchronous because the amount of 5' oligonucleotide marker (omega) recovered remained constant throughout a 15 min period in SDS. Additional RNase T1-sensitive oligonucleotides were exposed only after 1 to 2 min in SDS. Coat protein (CP) subunits released from virions 'destabilized' by ultracentrifugation at between pH 7.2 and 9.2 were quantified using L-[35S]methionine-labelled particles of TMV strain U2. CP recovery and virus particle translation results were consistent with increasing numbers of virions uncoating for approximately 200 nucleotides. In the presence of sparsomycin (SPN), the TMV strain vulgare 5' leader and the first AUG codon can bind two 80S ribosomes. Electron microscopy of pH 7.5-treated TMV particles incubated in SPN-treated wheatgerm extract or rabbit reticulocyte lysate, showed that approximately 10% of virions complexed with one ribosome and approximately 10% with two bound ribosomes, confirming that omega at least had been uncoated. Nucleocapsids in these complexes were shorter than untreated TMV by 9 to 10 nm (i.e. equivalent to 192 to 217 nucleotides exposed). The template activities of virions pretreated at pH 7.2 to 9.2 were destroyed by RNase H when short cDNAs were hybridized to sequences at, or immediately 3' to, the first AUG codon. We propose that the complete 5' leader of TMV RNA interacts weakly with CP subunits and that this micro-instability is due to the absence of G residues and is essential for initiation of cotranslational virus disassembly.
J Gen Virol 1991 Apr
PMID:Complete uncoating of the 5' leader sequence of tobacco mosaic virus RNA occurs rapidly and is required to initiate cotranslational virus disassembly in vitro. 184 66


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