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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We present evidence that the Escherichia coli DNA binding protein, IHF, plays an important role in conjugal transfer of the plasmid F. Our results suggest that IHF exerts this effect by positively effecting transcription of the transfer (tra) operon of the plasmid.
Mol Gen Genet 1987 May
PMID:Expression of F transfer functions depends on the Escherichia coli integration host factor. 330 98

We have shown that the plasmid pSC101 is unable to be maintained in strains of E. coli carrying deletions in the genes himA and hip which specify the pleitropic heterodimeric DNA binding protein, IHF. We show that this effect is not due to a modulation of the expression of the pSC101 RepA protein, required for replication of the plasmid. Inspection of the DNA sequence of the essential replication region of pSC101 reveals the presence of a site, located between the DnaA binding-site and that of RepA, which shows extensive homology with the consensus IHF binding site. The proximity of the sites suggests that these three proteins, IHF, DnaA, and RepA may interact in generating a specific DNA structure required for initiation of pSC101 replication.
Mol Gen Genet 1986 Jul
PMID:Replication of pSC101: effects of mutations in the E. coli DNA binding protein IHF. 352 58

A soluble enzyme system has been prepared from a phage P4-infected Escherichia coli strain that supports the replication of exogenous, supercoiled P4 DNA. This DNA synthesis in vitro depends upon the four deoxyribonucleotides and ATP, but is enhanced about four- to fivefold by the presence of other ribonucleotides. E. coli DNA polymerase III holoenzyme, the E. coli single-strand DNA binding protein, and the partially purified P4 alpha gene product are required for replication in vitro. Rifamycin does not inhibit P4 replication in vitro. Since the P4 alpha gene codes for a rifamycin-resistant RNA polymerase (Barrett et al., 1983), and since P4 DNA replication is independent of the host primase (Bowden et al., 1975), we believe the alpha gene product is functioning as a P4-specific DNA primase.
J Mol Biol 1985 Apr 20
PMID:The replication of bacteriophage P4 DNA in vitro. Partial purification of the P4 alpha gene product. 387 88

DNA binding proteins present in the cytoplasm and nuclei of term placenta were isolated by DNA-cellulose chromatography and analysed by electrophoresis in high resolution polyacrylamide gradient gels. A denatured DNA specific protein of approximate molecular weight 34 000 daltons was the predominant DNA binding protein of the cytoplasm; this protein consisted of over 65% of the total DNA binding proteins of the 0.15 M NaCl eluate of the cytoplasm. The cytoplasmic extracts contained two additional DNA binding proteins of molecular weight 24 000 and 18 000 daltons and these proteins bound preferentially to ds DNA. All the three DNA binding proteins were also present in the nuclei and electrophoresis of histones in adjacent lanes indicated that they are not histones. The 34 000-dalton DNA binding protein has been purified by ammonium sulphate fractionation followed by phosphocellulose (PC) chromatography. The DBP eluted from the PC column between 0.125-0.15 M potassium phosphate. PC fractions containing electrophoretically pure 34 KD DBP showed an endonuclease activity capable of converting plasmid pBR 322 DNA to the linear form. Maximum endonucleolytic activity was observed in the presence of 3-5 mM Mg2+ and the enzyme activity was completely inhibited by 3 mM ethylenediamine tetraacetate.
Mol Biol Rep 1984 Dec
PMID:DNA-binding proteins of human placenta: purification and characterization of an endonuclease. 609 9

We have developed a sensitive transient expression assay in 293 cells to study the effect of VA RNAs on the translation of adenovirus mRNAs. Monolayers of 293 cells were transfected with mixtures of recombinant plasmids encoding adenovirus-specific transcription units and plasmids encoding VA RNAs. Transfected cells were labeled with [35S]methionine for ca. 15 h, and labeled cell extracts were prepared. Changes in the protein expression caused by VA RNA cotransfection were measured by immunoprecipitation, using monospecific antisera prepared against adenovirus-specific polypeptides. Using this experimental design, we demonstrate that VA RNAI stimulates the translation of both early and late adenovirus mRNAs. Synthesis of the E3 19,000-dalton glycoprotein and the E2A 72,000-dalton DNA binding protein was stimulated between 10 and 20 times by VA RNAI cotransfection. Synthesis of the late hexon polypeptide was also stimulated, although translation of hexon was from an aberrant mRNA lacking the second and third segments of the common tripartite leader attached to late adenovirus mRNAs. VA RNAII, although very homologous to VA RNAI, does not function as a translational stimulator.
Mol Cell Biol 1984 Apr
PMID:Adenovirus VA RNAI: a positive regulator of mRNA translation. 620 22

Mutations affecting single-strand DNA binding protein (SSB) impair induction of mutagenic (SOS) repair. To further investigate the role of SSB in SOS induction and DNA repair, isogenic strains were constructed combining the ssb+, ssb-1 or ssb-113 alleles with one or more mutations known to alter regulation of damage inducible functions. As is true in ssb+ strains tif-1 (recA441) was found to allow thermal induction of prophage lambda + and Weigle reactivation in ssb-1 and ssb-113 strains. Furthermore, tif-1 decreased the UV sensitivity of the ssb-113 strain slightly and permitted UV induction of prophage lambda + at 30 degrees C. Strains carrying the recAo281 allele were also constructed. This mutation causes high constitutive levels of RecA protein synthesis and relieves much of the UV sensitivity conferred by lexA- alleles without restoring SOS (error-prone) repair. In contrast, the recAo281 allele failed to alleviate the UV sensitivity associated with either ssb- mutation. In a lexA1 recAo281 background the ssb-1 mutation increased the extent of postirradiation DNA degradation and concommitantly increased UV sensitivity 20-fold to the level exhibited by a recA1 strain. The ssb-113 mutation also increased UV sensitivity markedly in this background but did so without greatly increasing postirradiation DNA degradation. These results suggest a direct role for SSB in recombinational repair apart from and in addition to its role in facilitating induction of the recA-lexA regulon.
Mol Gen Genet 1983
PMID:DNA repair properties of Escherichia coli tif-1, recAo281 and lexA1 strains deficient in single-strand DNA binding protein. 622 44

Weigle reactivation and mutagenesis have been found to be defective in strains of E. coli deficient in single-strand DNA binding protein (SSB). These defects parallel those previously found in prophage induction and amplification of recA protein synthesis in ssb- strains. Together, these results demonstrate a role for SSB in the induction of SOS responses. UV survival studies of ssb- recA- and ssb- uvr- strains are presented which also suggest a role for SSB in recombinational repair processes but not in excision repair. Studies of host cell reactivation support this latter conclusion.
Mol Gen Genet 1981
PMID:DNA repair in E. coli strains deficient in single-strand DNA binding protein. 627 85

We have transduced the mutant allele ssb-1, which encodes a temperature-sensitive single-strand DNA binding protein (SSB), into several Escherichia coli strains, and have examined colony-forming ability, DNA replication, sensitivity to ultraviolet light (UV) and UV-induced mutability at the nonpermissive temperature. We have found: 1) that the degree of ssb-1-mediated temperature-sensitivity of colony-forming ability and of DNA replication is strain-dependent, resulting in plating efficiencies at 42 degrees C (relative to 30 degrees C) ranging from 100% to 0.002%; 2) that complete suppression of the temperature-sensitivity caused by ssb-1 occurs only on nutrient agar, and not in any other medium tested; 3) that strains in which ssb-1-mediated temperature-sensitivity is completely suppressed show moderate UV sensitivity and normal UV mutability at 30 degrees C, but much more extreme UV sensitivity and drastically reduced UV mutability at 42 degrees C; and 4) that defects in excision repair or in other Uvr+-dependent processes are not responsible for most of the UV sensitivity promoted by ssb-1. We discuss our results in relation to the known properties of SSB and its possible role in the induction of DNA damage-inducible (SOS) functions.
Mol Gen Genet 1981
PMID:Variable expression of the ssb--1 allele in different strains of Escherichia coli K12 and B: differential suppression of its effects on DNA replication, DNA repair and ultraviolet mutagenesis. 627 86

Seven mutations that affect various activities of the multifunctional DNA binding protein (DBP) encoded by human adenovirus have been physically mapped to different locations within DBP gene by marker rescue experiments. Two of these mutants (Ad5ts107 and Ad5ts125) contain a lesion which, under nonpermissive temperatures, decreases the capacity of the protein to bind single-strand DNA, blocks DNA replication, and prevents normal turn-off of viral early genes. In addition, the efficiency of transformation by the ts viruses compared to wild-type virus is increased at the nonpermissive temperature. Both ts mutations are located in the 3' half of the DBP gene (C-terminal half of DBP). In contrast, the alterations in the five host range mutants (Ad2hr400-Ad2hr403, Ad5hr404) which overcome the block to viral late mRNA synthesis in monkey cells, but have no marked effect on DNA replication or early gene expression map in the 5' half of the DBP gene. These results suggest that the 72 kd DBP of adenovirus contains at least two functionally separable domains.
J Mol Appl Genet 1982
PMID:Genetic evidence for separate functional domains on the human adenovirus specified, 72 kd, DNA binding protein. 628 27

Two herpes simplex virus proteins, the major capsid protein and the major DNA binding protein, are specifically localized to the nucleus of infected cells. We have found that the major proportion of these proteins is associated with the detergent-insoluble matrix or cytoskeletal framework of the infected cell from the time of their synthesis until they have matured to their final binding site in the cell nucleus. These results suggest that these two proteins may interact with or bind to the cellular cytoskeleton during or soon after their synthesis and throughout transport into the cell nucleus. In addition, the DNA binding protein remains associated with the nuclear skeleton at times when it is bound to viral DNA. Thus, viral DNA may also be attached to the nuclear framework. We have demonstrated that the DNA binding protein and the capsid protein exchange from the cytoplasmic framework to the nuclear framework, suggesting the direct movement of the proteins from one structure to the other. Inhibition of viral DNA replication enhanced the binding of the DNA binding protein to the cytoskeleton and increased the rate of exchange from the cytoplasmic framework to the nuclear framework, suggesting a functional relationship between these events. Inhibition of viral DNA replication resulted in decreased synthesis and transport of the capsid protein. We have been unable to detect any artificial binding of these proteins to the cytoskeleton when solubilized viral proteins were mixed with a cytoskeletal fraction or a cell monolayer. This suggested that the attachment of these proteins to the cytoskeleton represents the actual state of these proteins within the cell.
Mol Cell Biol 1983 Mar
PMID:Nuclear localization of herpesvirus proteins: potential role for the cellular framework. 630 71


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