Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Constitutive and interferon-inducible DNase hypersensitive sites in vivo are located in interferon-stimulated gene promoters near sequences that specifically bind constitutive or interferon-inducible proteins in vitro. Induced sites and proteins are transient or maintained, depending on cell type. Interferon-stimulated gene transcription is transient or maintained in parallel.
Mol Cell Biol 1989 Aug
PMID:In vivo evidence of interaction between interferon-stimulated gene factors and the interferon-stimulated response element. 279 95

An endo-exonuclease has been purified from logarithmically growing cells of the yeast Saccharomyces cerevisiae. Identification and purification of this nuclease was facilitated by its being precipitable with an antibody raised against a previously described Neurospora crassa endo-exonuclease (Resnick, M. A., Chow, T. Y.-K. Nitiss, J., and Game, J. C. (1984) Cold Spring Harbor Symp. Quant. Biol. 49, 639-649 and T. Y.-K. Chow and M. A. Resnick (1988) Mol. Gen. Genet., in press). The enzyme which was purified to near homogeneity was composed of a molecular weight 72,000 monomer. The single-strand nuclease activity is endonucleolytic and nonprocessive, whereas the double-strand DNase activity is exonucleolytic and weakly processive. Both nuclease activities have a pH optimum of 7.5, require Mg2+ or Mn2+ but not Zn2+ or Ca2+, are not inhibited by ATP, and exhibit the same kinetics of heat inactivation. Although this protein is not the product of the RAD52 gene, the greatly reduced amounts in rad52 mutants implicate the enzyme in repair and recombination processes in both mitotic and meiotic cells.
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PMID:Purification and characterization of an endo-exonuclease from Saccharomyces cerevisiae that is influenced by the RAD52 gene. 282 28

The distribution of capsid proteins induced by herpes simplex virus type 1 infection was determined at the ultrastructural level. The antiserum A to total capsid proteins and the anti-NC1 and NC2 sera, all labeled with gold particles, decorated the entire thickness of both empty capsids and nucleocapsids filled with viral DNA. On the other hand, an antibody to NC3,4 protein produced a heavy labeling concentrated almost entirely along the internal surface of empty capsids, whereas full capsids were not labeled. DNase digestion of "full" capsids did not restore anti-NC3,4 protein binding at this site. Published biochemical data concerning viral protein distribution in capsids are conflicting, but if NC3,4 protein is present in full capsids, we suggest that new binding forces between capsid proteins occurred at the time of insertion of viral DNA which might conceal the relevant antigenic sites of NC3,4 proteins. Capsid proteins were abundantly present in the viral nucleoplasm and in most constituents of the infected cells particularly some nucleoli and some but not all dense bodies. However, whereas anti-NC1 serum labeled nucleoli but not dense bodies, both anti-NC2 and anti-NC3,4 sera stained only dense bodies but not nucleoli. Inhibition of replication of viral DNA which entered the cell during the infective period did not inhibit the production of capsid proteins. Inhibition of protein synthesis in late infected cells did not alter the distribution of capsid proteins.
J Ultrastruct Mol Struct Res 1988 Mar
PMID:Involvement of nucleoli and dense bodies in the intranuclear distribution of some capsid polypeptides in cells infected with herpes simplex virus type 1. 284 85

The transposase protein and the inverted repeat sequences of Tn3 are both essential for Tn3 cointegrate formation and transposition. We have developed two assays to detect site-specific binding of transposase to the inverted repeats: (1) a nitrocellulose filter binding assay in which transposase preferentially retains DNA fragments containing inverted repeat sequences, and (2) a DNase 1 protection assay in which transposase prevents digestion of the inverted repeats by DNase 1. Both assays show that transposase binds directly to linear, duplex DNA containing the inverted repeats. The right inverted repeat of Tn3 binds slightly more strongly than the left one. Site-specific binding requires magnesium but does not require a high energy cofactor.
J Mol Biol 1988 Jun 05
PMID:Binding of the Tn3 transposase to the inverted repeats of Tn3. 284 51

We have examined the cell type-specific regulation of the human BK virus (BKV) enhancer. This enhancer functions efficiently in cis to activate expression from the adenovirus major late promoter in the human kidney cell line, 293, and in a monkey kidney cell line, MK2, but not in the HeLa cell line. In gel retardation migration assays, specific BKV enhancer-protein complexes could be observed by using nuclear extracts prepared from each cell line. Moreover, a unique DNA-protein complex was observed by using the HeLa cell nuclear extracts. By DNase footprint analysis, four binding regions for HeLa cell nuclear proteins were defined within the BKV enhancer repeat region. Two of the protected regions encompassed nuclear factor 1 or CCAAT transcription factor binding sites. These nuclear factor 1 sites also were protected by nuclear proteins from the 293 and MK2 cell lines. The other two protected sites encompassed a region of symmetry which included a sequence similar to the simian virus 40 TC enhancer motif and to a conserved sequence present upstream or within the introns of several cellular genes. These two sites were not protected by either the 293 or MK2 nuclear proteins. Competition studies in transfected cells indicated that the reduced activity of the BKV enhancer in the HeLa cell line was due to negative regulation. Further, we have demonstrated that binding of a nuclear factor(s) to the HeLa cell-specific site is involved in the repression of enhancer activity.
Mol Cell Biol 1988 Aug
PMID:Negative regulation of the human polyomavirus BK enhancer involves cell-specific interaction with a nuclear repressor. 285 Apr 93

The FLP recombinase interacts with its target sequence with the formation of three distinct DNA-protein complexes. The first complex leaves neither a DNase footprint nor is the DNA protected from methylation by dimethyl sulfate. We have found, however, that the FLP protein is bound predominantly to only one of the three 13 base-pair (bp) symmetry elements. This asymmetric loading of the FLP site seems to require the presence of an adjacent directly repeated 13 bp element. We speculate that this asymmetric filling of the target site may be accompanied by the unique order of cleavage and exchange of DNA strands.
J Mol Biol 1988 Nov 20
PMID:The mechanism of loading of the FLP recombinase onto its DNA target sequence. 285 60

The addition of tryptophan to adult rat hepatocyte cultures stimulated DNA synthesis. The increase in DNA synthesis as measured by 3H-thymidine incorporation into DNA was observed on treatment of the cultures with tryptophan for 48 h but also as short as for 6 h in comparison with control cultures. An increase was also apparent at 30 h which was maintained for up to 48 h post treatment with tryptophan. The increase in DNA synthesis by tryptophan cannot be attributed to cell injury or to increased DNA degradation. Of the degradative enzymes added after harvesting the hepatocytes, only DNase decreased incorporation of 3H-thymidine. The observed effect was specific for tryptophan since treatment with kynurenine, isoleucine, methionine or serine failed to show a significant effect. Pretreatment of cultured hepatocytes with hydroxyurea prevented the tryptophan stimulated increase in DNA synthesis suggesting that the latter was due to replicative and not to reparative DNA synthesis. Experiments performed with the addition of diethylnitrosamine also alluded to tryptophan's role in replicative DNA synthesis. The mechanism of tryptophan-induced DNA synthesis is discussed.
Virchows Arch B Cell Pathol Incl Mol Pathol 1987
PMID:Effect of tryptophan on isolated hepatocytes of rats. 288 59

The zen protein is encoded by the zerknullt gene required for normal early development in Drosophila. Like many regulatory proteins of this type, zen contains a 60 amino acid homeobox sequence. We have purified the zen protein and studied its solution behavior and its interaction with DNA. The zen protein exists as a monomer in solution with a molecular weight of about 40,000. It binds specifically to a site about 900 bases upstream from the zen gene. Within this binding site DNase protection experiments indicate that binding is confined to two regions approximately 11 and 14 bases in length that are separated by about 30 base pairs. The protein concentration dependence of the binding curve suggests that protein binding is non cooperative.
Mol Cell Biochem 1988 Feb
PMID:Purification and properties of the Drosophila zen protein. 289 36

A deviation from physiological osmolality (300 mOsm/kg H2O) can lead to genotoxic effects. A 30-min treatment of V79 hamster cells with hypotonic sodium chloride of 60 mOsm/kg H2O or with diluted culture medium of the same osmolality induces extraordinarily high frequencies of chromosomal aberrations. In this study, multiple fixation times over a 24-hr period were used to identify cells in various stages of the cell cycle at the time of treatment and to find out whether or not hypotonic conditions are able to induce aberrations in all cell cycle stages. Because of the aberration pattern observed, it is suggested that hypotonic treatment acts as an S-independent agent, like X-rays or restriction endonucleases. Whether the aberrations originate from directly induced DNA damage or from a release of DNase after lysosomal breakdown is discussed.
Environ Mol Mutagen 1989
PMID:Induction of chromosomal aberrations by hypotonic culture conditions is independent of the S-phase in V79 hamster cells. 291 Jul 3

A computer analysis of human and primate alphoid DNA was performed. The number and localization of short inverted complete repeats within alphoid DNA dimers (but not monomers) remain conserved. Thus, in spite of high heterogeneity of the primary structure the conserved secondary structure of alphoid DNA might be functionally important. The analysis of internal periodicity of the monomeric sequences of human and primate alphoid DNA revealed its potential ancient sequence, that is a simple satellite DNA with a reiterated heptanucleotide TGAAAAA, which is suggested to be the ancestor of satellite DNase of rodents. The facts reported propose the ancient origin and possible functional role of alphoid-like DNA as a universal pericentromeric superfamily of DNA.
Mol Biol (Mosk)
PMID:[Structural analysis of alphoid DNA of primates. II. Evolution and possible origin of alphoid DNA of primates]. 301 13


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