Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.30.2 (endonuclease)
18,621 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

All Bacillus subtilis R-type strains showing the phenomena of restriction and modification contain an endonuclease that inactivates in vitro the biological activity of a variety of DNAs lacking R-specific modification, such as transfecting SPPI, SPO2 and phi105 DNA, and transforming B. subtilis 168-type DNA. The corresponding DNAs carrying R-specific modification are resistant to the enzyme. The enzyme has been purified approximately 400-fold and is essentially free from contaminating double strand-directed unspecific exo- or endonuclease activity. Only Mg2+ is required as cofactor. The substrate DNAs are cleaved at specific sites. The double-stranded fragments produced from SPP1 DNA (molecular weight 2.5 x 10(7)) have an average molecular weight of about 3 x 10(5).
Mol Gen Genet 1975 Dec 30
PMID:Restriction and modification in B. subtilis. Purification and general properties of a restriction endonuclease from strain R. 0 56

Some physico-chemical properties of the DNAs released from the actinophages SH3, SH10, SH11, and SH12 are described. The four phage DNAs have a linear double-stranded secondary structure and are unique with respect to their high G.C contents which, from melting studies and buoyant density experiments, were found to be in the range of 68-73 mol-%. The DNA molecular weights were determined by sedimentation velocity experiments and by electron microscopic length measurements, the mean values of the two corresponding data sets being 34.0 x 10(6) (SH3), 26.7 x 10(6) (SH10), 26.1 x 10(6) (SH11), and 28.7 x 10(6) (SH12) with a mean relative error of +/- 5%. From different observations it was concluded that SH10 DNA, and possibly also SH11 and SH12 DNA, have cohesive ends and can undergo intramolecular or intermolecular association to form ring-like monomers or linear and ring-like multimers. Cleavage of the DNAs of SH3, SH10, SH11, and SH12 by EcoRI restriction endonuclease delivered two, one, zero, and two cleavage sites, respectively, and by BamHI restriction endonuclease eight, zero, zero, and zero cleavage sites, respectively.
Mol Gen Genet 1979
PMID:Molecular characterization of the genomes of actinophages SH3, SH10, SH11, and SH12 infecting Streptomyces hygroscopicus. 4 14

A highly efficient method for transformation of Bacillus subtilis by plasmid DNA is reported. The procedure, which involves polyethylene glycol-induced DNA uptake by protoplasts and subsequent regeneration of the bacterial cell wall, yields up to 80% transformants with an efficiency of 4 x 10(7) transformants per microgram of supercoiled DNA. Plasmids constructed by in vitro ligation or endonuclease-generated fragments of linear plasmid DNA can also transform PEG-treated protoplasts, but at a lower frequency.
Mol Gen Genet 1979 Jan 05
PMID:High frequency transformation of Bacillus subtilis protoplasts by plasmid DNA. 10 88

41 genes of SPP1 have been delineated by using complementation analyses of 75 conditionally lethal (ts and sus) mutations. The physical locations of these genes on the SPP1 chromosome have been determined by transfection/marker rescue experiments in which restriction endonuclease generated fragments of SPP1 DNA were used as donor DNA. The physical order of these fragments has been previously established (Ratcliff et al., 1979).
Mol Gen Genet 1979 Oct 01
PMID:The genome of B. subtilis phage SPP1: physical arrangement in phage genes. 11 20

The drug resistance genes on the r-determinants component of the composite R plasmid NR1 were mapped on the EcoRI restriction endonuclease fragments of the R plasmid by cloning the fragments using the plasmid RSF2124 as a vector. The sulfonamide (Su) and streptomycin/spectinomycin (Sm/Sp) resistance genes are located on EcoRI fragment G of NR1. The expression of resistance to mercuric ions (Mer) requires both EcoRI fragment H and I of NR1. The expression of chloramphenicol (Cm) and fusidic acid (Fus) resistance requires EcoRI fragments A and J of NR1. The kan fragment of the related R plasmid R6-5 can substitute for Eco RI fragment J of NR1 in the expression of Cm and Fus resistance. The structural genes for Cm and Fus resistance appear to be a part of an operon whose expression is controlled by the same promoter.
Mol Gen Genet 1978 Jan 17
PMID:Mapping of the resistance genes of the R plasmid NR1. 14 19

Salmonella ordonez (BM 2000) codes for kanamycin (Km, aphA), ampicillin (Ap), streptomycin (SmSp:aadA and Sm:aphC), chloramphenicol (Cm), tetracycline (Tc) and sulfonamide (Su) resistances and for production of colicin Ib (Cib). Genetical analysis by incompatibility testing, conjugation, transformation and physical studies using electron microscopy, agarose gel electrophoresis, led us to associate the Km and Cib characters to a 98.7 kilobase (kb) IncI1 plasmid (pIP565), and the Sm (aphC) and Su determinants to a 8.3 kb plasmid (pIP605). The ApCmSmSp(aadA)SuTc determinants were not associated in BM2000 S. ordonez with a plasmid structure. Following conjugation of S. ordonez to E. coli, the ApCmSmSpSuTc determinants were found stably associated with a single plasmid structure (pIP173, 127.5 kb) belonging to IncI1 group. Agarose gel electrophoresis of plasmid DNA restriction endonuclease digests and electron microscopy heteroduplex analysis showed that the acquisition of the ApCmSmSpSuTc determinants resulted from the insertion into pIP565 of a 28.8 kb DNA sequence. This sequence coding for ApCmSmSpSuTu resistances in S. ordonez could be translocated either to pIP565 plasmid or to several IncI1 plasmids but never to plasmids belonging to IncW, IncP or IncFII, suggesting the existence of specific sequences on the IncI1 receptor plasmids. Moreover, R-determinants were translocated back "en bloc" from pIP173 to the chromosome of a susceptible S. ordanez. The results were consistent with the presence in BM2000 S. ordonez chromosomal DNA of an integrated translocatable sequence encoding ApCmSmSpSuTc resistances. Such a structural association could account for the stability of these resistances in the Salmonella ordonez serotype.
Mol Gen Genet 1979 Jan 16
PMID:Reversible translocation of antibiotic resistance determinants in Salmonella ordonez. 15 72

The DNA homology relationships of 25 micrococci (15 strains of Micrococcus, eight strains of Sarcina and two strains of Staphylococcus) were studied by the deoxyribonucleic acid hybridization method using nuclease S1, an endonuclease specific for single-stranded DNA molecules. Nineteen of the strains were classified into three groups. Group I contained Micrococcus lysodeikticus IAMI056, M. luteus IAMI1010, M. flavus IAMI2005 and IAMI2006, Sarcina flava IAMI2007 and IAMI1006. S. subflava IAMI2009, S. lutea ATCC381, and ATCC382, and M. luteus IAMI1006. Group II contained M. roseus IAMI315, ATCC412, ATCC185 and IAMI295. Group III contained S. lutea IAMI099, IFO3232 and ATCC383, M. varians ATCC399 and Staphylococcus lactis ATCC15306. Micrococcus luteus IAMI097, M. varians ATCC19099 and ATCC19100, M. conglomeratus IAMI459 and IAMI470, and St. aureus IAMI011 could not be assigned to any of the three groups. The grouping corresponds to that derived from the results of differential lysis by lysozyme, 'lytic enzyme 2' from Cytophaga sp., or Streptomyces albus G enzyme; and to types of peptidoglycan in the cell walls and genetic transformation. The usefulness of classification based on sensitivity to various lytic enzymes was demonstrated. Group I probably coincides with M. luteus of Bergey's Manual of Determinative Bacteriology (1974), and groups II and III with M. roseus and M. varians respectively.
J Gen Microbiol 1976 May
PMID:Classification of micrococci on the basis of deoxyribonucleic acid homology. 18 Feb 38

It was found that yeast cells contain an endonuclease specific for apurinic sites in DNA which has no effect on DNA with normal strands or on strands with alkylated sites. The enzyme activity was studied in the RAD strain and in rad 6, rad 18-2 and rad 21 mutants, all very sensitive to MMS, as compared to the wild type. The level of endonuclease activity does not differ much between the tested strains, regardless of their differences in susceptibility to MMS. The enzyme activity is not induced by pretreatment of the cells with this mutagen.
Mol Gen Genet 1977 Jul 20
PMID:Endonuclease for apurinic sites in yeast. Comparison of the enzyme activity in the wild type and in rad mutants of Saccharomyces cerevisiae to MNS. 19 92

A characterization of a specialized transducing lambda phage for the deo operon (lambdaddeo), and some composite colE1-deo plasmids is given in this paper. This includes localization of the RSmaI, RHind/III, RBamI, and REcoRI sensitive sites. The deo genes have been localized by construction of composite colE1-deo plasmids. Using the DNA fragments, obtained by digestion with REcoRI and RHindIII, respectively, as templates in an in vitro protein synthesizing system, it has been possible to give the direction of transcription and the exact location of the deo genes, relative to the endonuclease sites. Furthermore, the cytO,P and deoO,P regions have been mapped relative to the structural genes. Supercoiled co1E1-deo DNA has been used as template in the in vitro system; this DNA gives essentially the same results as the endonuclease-fragmented DNA. The use of the different types of templates is discussed.
Mol Gen Genet 1977 Sep 21
PMID:On the structure of the deo operon of Escherichia coli. 20 Aug 36

A new set of hybrid viruses has been isolated whose closed circular genomes 5 to 6 kB in size, contain DNA sequences derived in part from adenoviruses 2 and in part from SV40. The structure of these genomes is complex, but in the simplest case, analyses by restriction endonuclease digestion and hybridization indicate that the adenovirus 2 DNA is present as a continuous block, of maximum size 2.8 kB. Different hybrids contain sequences derived from different segments of the adenovirus 2 genome.
J Gen Virol 1978 Feb
PMID:The isolation of defective variants of simian virus 40 whose genomes contain sequences derived from adenovirus 2 DNA. 20 54


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