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

The size and degree of homogeneity of the repetitive units in purified ribosomal DNA (gamma DNA) from Saccharomyces cerevisiae have been analyzed by restriction endonuclease digestion and heteroduplex mapping. Digestion of the gamma DNA with EcoRI yields seven fragments, digestion with Hind II+III yields five fragments, digestion with Hind III alone yields two fragments, and digestion with Sma I yields one fragment. The sum of the fragment molecular weights after digestion with each of the endonucleases is 5.5-5.6 x 10(6). When the DNA strands of the Sma I fragment are dissociated and reannealed, only homoduplexes are formed. We have concluded from these results that the repeating units in yeast ribosomal DNA are 5.6 x 10(6) datons and are homogeneous in size and composition.
Mol Gen Genet 1976 Nov 17
PMID:Restriction endonuclease analysis of ribosomal DNA from Saccharomyces cerevisiae. 79 60

The 2 micron circular DNA from S. cerevisiae has been cloned on bacteriophage lambda. The two forms of circular DNA which exist in equilibrium due to recombination between inverted repeat sequences were separated as stable clones, and a map of targets for restriction endonucleases EcoRI, HindIII and HpaI was constructed. The circular DNAs isolated from a particular oligomycin resistant strain and its parent oligomycin snesitive strain were compared by restriction endonuclease analysis, and no difference was detected. The potential uses of cloned 2 micron DNA in determining the possible biological role of these plasmids are considered.
Mol Gen Genet 1976 Nov 17
PMID:A map of the restriction targets in yeast 2 micron plasmid DNA cloned on bacteriophage lambda. 79 64

The 1400 base pair repeat produced by digestion of calf satellite I DNA (phi = 1.714 g/cm3) with EcoRI, was cloned in E. coli. The hybrid plasmid (pGM 214) which contains the ColE1-Ap vector (pSF 2124) and the 1400 base pair fragment replicates stably in E. coli and can be amplified by chloramphenicol treatment. No clone was found in which more than one "repeat unit" of the satellite I DNA was present in the chimaera plasmid. Digestion of the original satellite I and the plasmid pGM 214 with R-SmaI shows that the satellite DNA replicated in E. coli is cleaved by the restriction endonuclease SmaI whereas the original satellite I DNA from calf thymus is not, suggesting that the satellite I contains a large amount of modified cytosine or guanosine, probably 5-methyl-cytosine. R-EcoRI* produces a number of fragments with the satellite I in the range of 300 base pairs to 1400 base pairs. A physical map of pGM 214 (and pSF 2124) with R-EcoRI, R-HincII, R-HindIII, R-SmaI, R-BamI and R-EclI was constructed. The 1400 base pair "repeat unit" in the pGM 214 is efficiently transcribed in vitro by purified RNA polymerase, starting from a pSF 2124 promoter. The restriction enzyme EclI produces a 350 base pair repeat with calf satellite II (phi = 1,722 g/cm3), whereas the satellite I is not cut by this enzyme.
Mol Gen Genet 1976 Nov 24
PMID:Cloning of calf thymus satellite I DNA in Escherichia coli. 79 69

The relationship between the electrophoretic mobility of double stranded DNA fragments electrophoresed in agarose gel and their molecular weights within the range from 1.10(6) to 8.10(7) daltons and agarose concentration 0.3--2.0% has been studied. Partial hydrolysis products of lambda phage DNA obtained by restriction endonuclease EcoRI have been separated. Partial hydrolysis products have been identified by determining the fragments of full cleavage as well as by genetic methods using a system of transformation of E. coli cells treated with CaCl2, which have been infected with different helper-phages containing definite gene mutations.
Mol Biol (Mosk)
PMID:[Identification of partial hydrolysis products of lambda bacteriophage DNA by restriction endonuclease EcoRI]. 80 74

The enzymes involved in host-controlled modification and restriction by Bacillus subtilis strain N were detected in cell free extracts. In the presenct of Mg2+ the N-specific endonucleases cleaved unmodified DNA but did not attack phi-105C. N DNA carrying N-specific modification. The restriction endonuclease required neither SAM nor ATP for its activity. The N-specific modification enzyme was active only in the presence of SAM, indicating that modification in this syteem is a methylation of DNA.
Mol Gen Genet 1975 Jul 10
PMID:In vitro modification and restriction of phage phi-105c DNA with Bacillus subtilis N cell-free extract. 80 94

Restriction endonuclease R from Bacillus subtilis strain R cleaves nonmodified SPP 1 DNA in approximately 80, and lambda DNA in about 200 different sites. DNA digests with this endonuclease and with endonuclease Hae III from Haemophilus aegyptius show identical fragmentation patterns on gel electrophoresis, indicating that the two enzymes recognise the same nucleotide sequence. The polynucleotide kinase reaction was used in conjunction with two-dimensional ionophoretic nucleotide mapping methods to identify the 5'-nucleotide sequences at the sites of cleavage by the B. subtilis restriction endonuclease. The results show that the recognition sequence is (see article) where arrows indicate the points of strand scission. Each of the four possible nucleotides can occur in the positions flanking the recognition site.
Mol Gen Genet 1975 Dec 30
PMID:Restriction and modification in B. subtilis. Nucleotide sequence recognised by restriction endonuclease R. Bsu R from strain R. 81 3

It is known that DNA from phage T7 is not cleaved by restriction endonuclease EcoRI. However, DNA from phage T7am28 (gene 5) mutant (Studier, 1969) was found to be cleaved by the endonuclease at one site. The site is located at 0.46 fractional length from the left end of the molecule. The mutation which makes T7 DNA sensitive to the endonuclease is separable from the amber nutation and located between am28 and am233 (gene 6).
Mol Gen Genet 1977 Jan 18
PMID:EcoRI-sensitive mutation of T7 phage. 84 Feb 25

An endogenous Ca2+, Mg2+-dependent factor of enzymic nature (apparently an endonuclease) digests a part of chromatin in the rat liver nuclei producing DNA fragments of an uniform size. After 60 min of incubation at 15 degrees C and pH 7.50 in the presence of 5 mM MgCl2 and 2 mM CaCl2 87-93% of the total chromatin becomes soluble. The insoluble chromatin however contains 70-85% of the in vivo newly synthesized RNA. In regenerating liver the proportion of the insoluble residual chromatin increases while the radioactivity of the newly synthesized DNA in this fraction is highest. Residual chromatin can be solubilized by ultrasonic treatment only. The Ca2+, Mg2+-dependent dissolving factor is not present either in brain or in PMN leucocyte nuclei.
Mol Biol (Mosk)
PMID:[Solubilization of chromatin by an endogenous enzymic Ca2+, Mg2+-dependent factor. Activity of residual chromatin]. 105 86

Replicating DNA molecules of a deletion mutant of the conjugative R-plasmid R 6 K are cleaved at a single site by the EcoRI restriction endonuclease. Electron microscope examination and measurements of the EcoRI treated replicative intermediate molecules indicate that replication can be initiated at two sites on the plasmid DNA molecule. The two sites are located at about 23 and 39% of total length, respectively, from the EcoRI cleavage site. About 5% of the replicating molecules use both replication initiation sites simultaneously.
Mol Gen Genet 1975 Sep 15
PMID:Two replication initiation sites on R-plasmid DNA. 110 50

A soluble extract prepared from T7-infected E. coli is able to initiate DNA synthesis on an exogenous T7 DNA template. We have developed a fractionation procedure to resolve and identify the proteins required for T7 DNA synthesis. By this method we have purified the following T7 replication-related proteins (each greater than 50% pure as judged by sodium dodecyl sulfate gel electrophoresis): T7 DNA-binding protein (27,000 daltons), T7 RNA polymerase (105,000 daltons), T7 DNA polymerase (gene 5-protein, 85,000 daltons, plus host-factor), T7 DNA ligase (40,000 daltons), and T7 DNA-priming protein (65,000 daltons). The T7 DNA-priming protein, synthesized between 7.5 and 15 min following infection, was not detectable if the infecting phage carried an amber mutation in gene 4. Using an in vitro complementation assay which specifically measures the stimulation of DNA synthesis in an extract prepared from T7 gene 4-mutant infected cells, we have purified the DNA-priming protein about 2,000-fold. The purified priming protein preparations are essentially free of endonuclease, exonuclease, DNA ligase and DNA polymerase activity, but they do contain measurable DNA-dependent RNA synthetic acitvity. The enzyme is rapidly inactivated by heating to 46 degrees C and by treatment with N-ethylmalemide. In the presence of T7 DNA-binding protein and all four ribonucleoside triphosphates, the DNA-priming protein enables T7 DNA polymerase to initiate DNA synthesis on intact duplex T7 DNA. Closer studies of its enzymatic function as well as of the possible roles of the other proteins in the T7 replication system will be presented in the accompanying paper.
Mol Gen Genet 1975 Dec 01
PMID:Studies on bacteriophage T7 DNA synthesis in vitro. I. Resolution of the T7 replication system into its components. 110 17


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