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Query: UMLS:C0001486 (Adenovirus)
 3,125 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Adenovirus-associated virus (AAV) structural proteins (VP1, VP2, and VP3) have been examined to determine if areas of sequence homology exist between these three virion proteins. Tryptic and chymotryptic maps have been produced which demonstrate extensive areas of sequence homology common to all three proteins. The amino acid compositions of the proteins were also determined and were found to be very similar. These data are consistent with the hypothesis that all three virion proteins arise either from a common precursor of similar transcripts.
J Gen Virol 1979 Oct
PMID:Adenovirus-associated virus structural protein sequence homology. 23 Mar 1

Polyriboinosinic acid (poly I) inhibits initiation of transcription by binary complexes formed between Adenovirus 2 DNA and E. coli RNA polymerase holoenzyme. In the presence of poly I, just as in the presence of rifampicin, initiation of transcription exhibits a sigmoidal dependence on the temperature at which the binary complexes are formed. This indicates that I (closed) complexes between Ad 2 DNA and RNA polymerase are rapidly inactivated by poly I, but that RS (open) complexes are relatively resistant. However, even among the RS complexes, at least two classes can be distinguished on the basis of the degree to which they are resistant to poly I: RS-1 complexes are somewhat sensitive to poly I (half-time of inactivation approximately 10 min) while RS-2 complexes are almost completely resistant to the inhibitor (half-time of inactivation approximately 10 h). For both types of RS complex, the degree of sensitivity to poly I is ionic strength-dependent.
Mol Gen Genet 1979 May 23
PMID:Inactivation of E. coli RNA polymerase by polyriboinosinic acid: heterogeneity of RS complexes. 38 42

Adenovirus DNA-protein complex purified by sedimentation on a sucrose gradient containing 4 M-guanidine hydrochloride was found to contain other virion proteins in addition to the terminal protein of mol. wt. 55000. In this report, we describe a simple and rapid method for the isolation of a homogeneous DNA-protein complex. The procedure involves gel electrophoresis of the complex on agarose in the presence of sodium dodecyl sulphate. DNA was found to migrate into the gel with a single protein of mol. wt. 55000 tightly attached to it. Restriction enzyme cleavage analysis of the DNA-protein complex shows that the protein is associated with the two terminal fragments.
J Gen Virol 1979 Nov
PMID:Isolation and characterization of a homogeneous DNA-protein complex from adenovirus type 2 virion. 54 68

Adenovirus type 5 DNA has low infectivity (Graham & van der Eb, 1973) which can be increased by various techniques, one of which is the dimethyl sulphoxide (DMSO) boost (Stow & Wilkie, 1976). In this report, it is shown that DMSO treatment of adenovirus 5 DNA-infected HeLa cells results in a 10-fold increase in plaque formation, and that this can be used to facilitate marker rescue experiments. Double DNA infections were performed by the calcium phosphate method, co-precipitating intact temperature-sensitive mutant DNA with purified wild-type DNA restriction endonuclease fragments. Analysis of the plaquing ability of these mixtures and any progeny virus has resulted in the assignment of six temperature-sensitive mutations to discrete physical locations on the adenovirus type 5 genome. These locations are discussed with respect to the mutant phenotypes and the transcription-translation products of the appropriate regions.
J Gen Virol 1978 Dec
PMID:Mapping of adenovirus type 5 temperature-sensitive mutations by marker rescue in enhanced double DNA infections. 74 9

E coli RNA polymerase holoenzyme is able to recognize transcription initiation sites on Adenovirus 2 DNA that are functionally indistinguishable from promoters for the enzyme on phage DNAs. The complexes formed between the polymerase and the DNA at these sites can exist in two states-either as I (initiation) complexes, from which rapid RNA chain initiation is not possible, or as RS (rapid starting) "rifampicin resistant" complexes, from which rapid RNA chain initiation can occur. When transcription is limited to that initiated from stable, rifmapicin-resistant pre-initiation complexes, initiation is strictly dependent on the presence of sigma factor; in addition, the frequency of initiation exhibits sigmoidal dependence on the temperature at which pre-initiation complexes are allowed to form, with a transition temperature of 26-28 degrees C. The average half-time for initiation of RNA chains from sites on Ad 2 DNA is shown to be comparable to half-times for initiation of RNA chains from promoters on T7 and lambda DNAs. At saturating levels of enzyme, the half-times are 0.6, 0.9, and 1.6 sec for lambda b2, Ad 2 and T7 DNAs, respectively. The existence of efficient, phage-like promoters for E coli RNA polymerase on Ad 2 DNA suggests to us that such promoters may be closely related functionally and spatially to promoters for mammalian RNA polymerases.
Mol Gen Genet 1976 Jan 16
PMID:I.n vitro transcription of adenovirus 2 DNA. I. Characterization of promoters for E. coli RNA polymerase. 76 51

We estimate that E. coli RNA polymerase is able to form stable, rifampicin-resistant, pre-intiation complexes with Adenovirus 2 DNA at three to six binding sites. The number of RNA chains initiated from such complexes has been determined form the incorporation of gamma-32P-ATP and -GTP at two rifampicin concentrations (7 mug/ml and 24 mug/ml) and after pre-incubation at either 25 or 37 degrees C. The total number of RNA chains initiated ranges from 2.6 per Ad 2 DNA molecule at a rifampicin concentration of 24 mug/ml and pre-incubation temperature of 25 degrees C, to 5.4 per Ad 2 DNA molecule at a rifampicin concentration of 7 mug/ml and pre-incubation temperature of 37 degrees C. Efficient initiation with GTP occurs only after pre-incubation at 37 degrees C whereas initiation with ATP is equally as efficient at either pre-incubation temperature. Promoters for initiation with ATP have been localized to the leftmost 58% of the Ad 2 DNA molecule, defined by the EcoR.RI restriction endonuclease fragment A; promoters for initiation with GTP are located on the remaining 42% of the Ad2 DNA molecule. It is likely that on Adenovirus 2 DNA each RNA chain is initiated from a unique binding site which constitutes a seperate promoter for E. coli RNA polymerase.
Mol Gen Genet 1976 Jan 16
PMID:In vitro transcription of adenovirus 2 DNA. II. Quantification and localization of promoters for E. coli RNA polymerase. 76 52

Adenovirus type 5 'cores' prepared by heating in the presence of deoxycholate and partially purified on a glycerol density gradient could be visualized as roughly isometrical particles with a condensed centre from which twisted filaments or loops of DNA emanated. This compact structure was readily dispersed by spreading on distilled water or by treatment with EDTA, Nonidet, DNase or trypsin. Spreading with Nonidet was particularly effective in unfolding the cores and revealing long filaments about 100 A thick presumably of the virus nucleoprotein. Subunits (about 30 to 60 A in diam.) could be seen free in the DNase-treated cores, suggesting a particulate nature of one or both of the core proteins.
J Gen Virol 1975 Jul
PMID:Electron microscopy of adenovirus cores. 80 87

Adenovirus type 2 cores can function effectively as templates in an in vitro replication system. Viral DNA replication assays using cores as templates do not differ in their requirements to the well characterized assays using DNA-complex templates, i.e. there is a dependence on terminal protein precursor (pTP), DNA polymerase and DNA binding protein and the assay is greatly stimulated by certain host transcription factors. The products of initiation and limited elongation are easily distinguishable and, in the system described, there is specific proteolysis of the pTP adducts as a function of the adenovirus-coded protease, present in the nuclear extracts from infected cells, or the core templates. Substitution of Mn2+ ions for Mg2+ ions in the replication assay has a dramatic effect on the nature of the replication events, in most cases resulting in the stimulation of initiation without elongation. Similar results can be achieved by utilizing subviral particles as templates, obtained by dialysis of purified adenovirus in a hypotonic buffer at pH 6.4. Restriction enzyme analysis of the replicated products confirmed that DNA synthesis proceeds from the adenovirus termini using both the core and subviral templates. By adding an ATP-regenerating system elongation can be further stimulated, particularly in the case of the subviral templates. Quantification of nucleotide incorporation into the appropriate restriction fragments indicates that for the subviral templates replication can proceed for at least 2000 to 3000 bases from either terminus. These results suggest that the adenovirus genome is packaged in the virion in a conformation readily available for at least the initial replication events. Such a conformation might also be appropriate for early transcription.
J Gen Virol 1989 Dec
PMID:Adenovirus subviral particles and cores can support limited DNA replication. 260 37

Adenovirus type 5 (Ad5) mRNAs present in cells transformed with left-terminal Ad5 DNA fragments (XhoI-C, 0 to 15.5%; HindIII-G, 0 to 7.7%; HpaI-E, 0 to 4.3% were characterized by 'Northern blotting' and S1 nuclease analysis. They were compared with the mRNAs transcribed from the Ad5 E1 region in the early and late stages of lytic infection. It is shown that in XhoI-C-transformed cells the same mRNAs were transcribed as early during lytic infection: two co-terminal mRNAs from region E1a, differing only in their splicing, and one major E1b transcript. In HindIII-G-transformed cells additional E1a mRNAs were detected with a novel 5' terminus, but with the normal splicing pattern. Instead of the normal E1b mRNA, HindIII-G-transformed cells were found to contain mRNAs consisting of a viral E1b segment and a non-viral segment. This E1b-encoded segment was shown not to be involved in RNA splicing. The mRNAs in cells transformed with Ad5 HpaI-E were similar to the E1a mRNAs found in XhoI-C- and HindIII-G-transformed, and in lytically infected cells but had aberrant 3' termini. These results are discussed in the light of the Ad5 E1 DNA and RNA sequences, and protein mapping data.
J Gen Virol 1983 May
PMID:Analysis of virus-specific mRNAs present in cells transformed with restriction fragments of adenovirus type 5 DNA. 630 9

Adenovirus type 5 ts mutants deficient in hexon metabolism were investigated using conformation-specific monoclonal antibodies directed against hexon capsomeres and the viral 100K protein. The ts mutants map either in the hexon structural gene or in the gene encoding the 100K protein, a major, late nonstructural protein. All of the mutants examined (ts1, ts2, ts3, ts4, ts17, and ts20 of J. F. Williams, M. Gharpure, S. Ustacelebi, and S. McDonald (1971). J. Gen. Virol. 11, 95-101) were unable to produce the capsomeric form of hexon (a trimer of three hexon monomers) at the nonpermissive temperature. However, all of the mutants retained the ability to produce a complex of 100K and hexon which has been demonstrated to play a major role in the assembly of hexon trimers. The mutants accumulated nontrimerized hexon in this ts complex in the perinuclear region of the cell. Several of the mutants (ts1, ts2, ts3) were found to successfully assemble hexon synthesized at the nonpermissive temperature upon shift down to the permissive temperature, even in the presence of a protein synthesis inhibitor. The mutant, ts2, which maps in the hexon structural gene, was found to be dependent on protein synthesis for transport of hexon trimers into the nucleus during temperature shift down, while the 100K ts mutants, ts1 and ts3, were independent of protein synthesis for both hexon assembly and transport.
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PMID:Analysis of Ad5 hexon and 100K ts mutants using conformation-specific monoclonal antibodies. 661 96


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