Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.21.3 (deoxyribonuclease)
1,528 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Transformation (i.e., DNase-sensitive genetic transfer) of strains of Streptococcus mutans representing serotypes c and e was accomplished by using chromosomal DNA from a Rifr Strr Spcr isolate of strain GS5 (UAB525) and a chimeric plasmid, pYA629. Shuttle plasmid pYA629 comprises the S. mutans plasmid pVA318, an inducible erythromycin resistance determinant originally isolated from a group A streptococcal strain, the tetracycline resistance gene and replication region of the Escherichia coli plasmid pBR322, and the promoter region of the S. mutans gene for aspartate beta-semialdehyde dehydrogenase. The strains examined for recipient ability included those known to lack a cryptic plasmid (GS5, UA130, UA159, and MT8148) and those known to contain a widely disseminated 5.8-kilobase cryptic plasmid (LM7, V318, UA101, UA174, and 3098791). The transformation frequencies in GS5 for GS5 chromosomal antibiotic resistance markers were comparable to those reported by others, but UA101, UA130, UA159 and UA174 were transformed with both chromosomal and plasmid markers at much higher efficiencies. In a larger strain survey, strains containing the 5.8-kilobase cryptic plasmid were more frequently transformable with both chromosomal and pYA629 DNAs than were strains lacking this cryptic plasmid. All plasmid-containing strains except LM7 lost their resident cryptic plasmids when transformed with pYA629. LM7 transformed with pYA629 retained pLM7. There are therefore at least two incompatibility groups among S. mutans cryptic plasmids. yPA629 DNA isolated from either E. coli or S. mutans transformed S. mutans with equal efficiency. pYA629 DNA isolated from S. mutans transformed both restriction-deficient and restriction-proficient E. coli recipients. Therefore, the strains of S. mutans used lack a restriction-modification system for pYA629 DNA sequences. S. mutans strains that are readily transformable, display maximal cariogenicity in gnotobiotic rats, and give high scores for in vitro measures of important virulence attributes have been identified to facilitate studies on the genetic basis and control of virulence.
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PMID:Transformation of Streptococcus mutans with chromosomal and shuttle plasmid (pYA629) DNAs. 302 26

Replacement of the amino-terminal 40-amino-acid region of the 588-amino-acid precursor of the membrane-bound penicillin-binding protein 3 (PBP3) by the decapeptide MKGKEFQAWI was carried out by altering the amino-coding end of the ftsI gene. Insertion of the modified gene into a runaway-replication plasmid under the control of a fused lpp promoter and lac promoter/operator, resulted in the overexpression by Escherichia coli of the modified PBP3 (designated PBP3**) in the cytoplasm. About 80% of the accumulated PBP3** underwent sequestration in the form of insoluble protein granules that were isolated by cell breakage or cell lysis. After selective removal of contaminants by an EDTA-lysozyme/DNase (deoxyribonuclease)/Nonidet extraction, treatment of the granules with guanidinium chloride followed by dialysis against buffer containing 0.5 M NaCl yielded a refolded, water-soluble PBP3**, which, upon chromatography on Superose 12, exhibited the expected 60,000 molecular mass. The refolded PBP3** bound benzylpenicillin in a 1 to 1 molar ratio, was highly sensitive to aztreonam and showed the same degree of thermostability, in terms of penicillin-binding capacity, as the parent, membrane-bound PBP3, suggesting that protein refolding occurred with formation of the correct intramolecular interactions. Two to three mg of refolded PBP3** can be obtained from 1 litre of culture of the overproducing strain.
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PMID:Overexpression, solubilization and refolding of a genetically engineered derivative of the penicillin-binding protein 3 of Escherichia coli K12. 305 Mar 60

A deoxyribonuclease was partially purified from the free-living nematode Caenorhabditis elegans. The DNase functioned as an endonuclease and introduced both single-strand nicks and double-strand breaks into DNA. The enzyme hydrolyzed double-stranded DNA seven times more rapidly than single-stranded DNA. DNase activity was not affected by the addition of divalent cations below 1 mM but was inhibited at higher ionic concentrations. In addition, the enzyme was not inhibited in the presence of 10 mM EDTA. The enzyme was inhibited by salt concentrations greater than 20 mM. Three independent mutations in the nuc-1 gene were shown to reduce nuclease activity to less than 1% of that seen in wild-type organisms.
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PMID:An endonuclease from Caenorhabditis elegans: partial purification and characterization. 322 46

All recB(-) and recC(-) mutants of E. coli carry out significant residual genetic recombination, whereas all recA(-) mutants form no recombinants. This observation suggests that an alternative minor pathway of recombination, independent of recB(+) and recC(+) products, may be operative in Escherichia coli. Rec(+) revertants of recB(-)recC(+), recB(+)recC(-), and recB(-) strains of E. coli have been isolated and are shown to fall into at least two major genotypic classes. One class carries revertant mutations which map in or very near the recB and recC genes. In this class an ATP-dependent DNase characteristic of wild type E. coli is restored. The reversions in this class are probably back-mutations or intragenic suppressor mutations. A second class carries revertant mutations which are located far from the recB and recC genes. In this class there is a high level of DNase activity which does not require ATP and is inactive on T4 DNA. Indirect and not informational suppression appears to be responsible for the second class of revertants. The suggestion is made that restoration of recombination by indirect suppression involves an activation or derepression of one or a series of enzymes, which participate in a pathway of recombination, alternative to the recB and recC pathway, but normally of minor importance. The ATP-independent DNase may be one of these enzymes.
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PMID:Biochemical and genetic studies of recombination proficiency in Escherichia coli. II. Rec+ revertants caused by indirect suppression of rec- mutations. 424 56

An ATPase activity that is completely dependent on DNA is associated with the ATP-dependent DNase (recB-recC enzyme) purified from Escherichia coli. There is a strong correlation between the ATPase and the DNase activities under various assay conditions. With E. coli DNA as substrate, 8-9 molecules of ATP are hydrolyzed to ADP and inorganic phosphate for every phosphodiester bond hydrolyzed by the DNase. The possible functional relationship of the ATPase and DNase activities is discussed.
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PMID:Adenosine triphosphatase associated with adenosine triphosphate-dependent deoxyribonuclease (recB-recC enzyme-E. coli-ATP to phosphodiester hydrolysis ratio-DNA-dependent ATPase activity). 425 17

After dissociation of the E. coli recBc DNase (ATP-dependent DNase) with concentrated NaCl, two subunit proteins were isolated by ion exchange chromatography. Combination and subsequent incubation of the subunits resulted in the appearance of the original DNase. The subunit proteins, designated alpha and beta, have s(20,omega) of 4.1 S and 8.1 S, respectively. The alpha subunit possesses neither the ATP-dependent Dnase nor the DNA-dependent ATPase of the original enzyme. The beta subunit contains a low level of both enzymatic activities in a ratio markedly different from that of the original enzyme. The beta subunit complemented extracts from both recB and recC mutant strains to produce recBC DNase, while the alpha subunit did not complement either extract. These results suggest that recB and recC genes are both required for the production of beta subunit and that the recBC DNase molecule contains a protein component (alpha) that is not determined by either the recB or the recC gene.
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PMID:The recBC deoxyribonuclease of Escherichia coli: isolation and characterization of the subunit proteins and reconstitution of the enzyme. 428 72

A technique is described for isolation of plasmid DNA in closed and open circular double-stranded forms from bacterial cells, by use of ATP-dependent deoxyribonuclease purified from Micrococcus luteus. This DNase, acting only upon linear DNA molecules, degrades all bacterial chromosomal DNA extracted in the linear form. Circular plasmid DNAs are left intact, and are then separated by sedimentation through a sucrose gradient. Unlike previous techniques for analysis of plasmid DNA, this technique can be used to isolate not only closed circular DNA but also open circular DNA. Several plasmids, such as those from phage (lambdadv1 and lambdadv21), a colicinogenic factor (Col E2), a sex factor (F(8)' gal), and "minicircles" in Escherichia coli 15, in both the open and closed circular forms, were well separated from chromosomal DNA by this technique.
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PMID:Isolation of circular DNA molecules from whole cellular DNA by use of ATP-dependent deoxyribonuclease. 435 70

DNA isolated from Mycoplasmatales viruses MVL51 and MVGs51 was infectious when mixed with Acholeplasma laidlawii BN1-Na1(R) cells. Infectivity was destroyed by deoxyribonuclease but not by ribonuclease, Pronase, or specific antiserum to the virus. Host mycoplasma cells were only competent for transfection during late-log growth phase. The rates of the establishment of DNase insensitivity of viral DNA transfectants were similar to those of bacteriophage systems. The dose-response curve for transfection suggested that an average of six molecules of DNA must interact with a cell in order to produce one infectious center. Mycoplasmatales virus DNA exhibited a low efficiency of infection; one infectious center required 4 x 10(5) virus equivalents of DNA.
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PMID:Transfection mediated by Mycoplasmatales viral DNA. 450 32

The ATP-dependent DNase activity of Escherichia coli disappeared or was markedly reduced after infection with double-stranded DNA phages, T2, T3, T4, T5, T6, T7, lambda, phi80, and P1, but not with the single-stranded DNA phage f1, or the RNA phage Qbeta. This DNase activity was not reduced when chloramphenicol was added prior to phage infection.
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PMID:Inactivation of the ATP-dependent DNase of Escherichia coli after infection with double-stranded DNA phages. 461 Jan 90

A deoxyribonuclease derived from Epstein-Barr virus (EBV)-producing lymphoblastoid cell line (NPC-204 cells) treated with IUdR was purified by DEAE cellulose, phospho-cellulose, and DNA-cellulose columns with 45% recovery. The activity of the DNase was neutralized by serum of patient with nasopharyngeal carcinoma (NPC). The DNase had a strong requirement for divalent cations and an alkaline pH optimum. Its activity was inhibited by highly ionic strength and polyamines.
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PMID:Activity of DNase associated with replication of Epstein-Barr virus in NPC-204 cells. 609 87


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