Biological Sciences: Non-specific ‘pairing’ of DNA molecules by recombination enzyme of Bacillus subtilis

Ohi, Seigo; Bastia, Deepak; Sueoka, Noboru

doi:10.1038/248586a0

Cited by 8 publications

(2 citation statements)

References 21 publications

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“…They have suggested that these large DNA fragments might participate as intermediates in the recombination process. Ohi et al (18) provided some evidence that the ATP-dependent DNase of B. subtilis brings DNA molecules into close proximity. They suggested that this property of the enzyme might have some relevance to the mechanism of recombination.…”

Section: Discussionmentioning

confidence: 99%

Effect of adenosine 5'-triphosphate-dependent deoxyribonuclease deficiency on properties and transformation of Haemophilus influenzae strains

Kooistra¹,

Venema²

1976

J Bacteriol

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A transformation-deficient strain of Haemophilus influenzae, lacking adenosine 5'-triphosphate-dependent deoxyribonuclease activity, was isolated by selection for sensitivity to mitomycin. The mutant, designated JK57, possibily showed a moderate sensitivity to ultraviolet (UV) irradiation and treatment with methyl methane sulfonate. Contrary to the wild type, the mutant degraded chromosomal deoxyribonucleic acid (DNA) to some extent. However, after UV irradiation to the mutant degraded considerably less DNA than the wild type and the TD24 mutant of H. influenzae, the latter being equivalent to a recA mutant of Escherichia coli. A TD2457 double mutant, constructed by transferring the TD24 mutation into the JK57 strain, was as sensitive to deleterious agents and as deficient in transformation as the TD24 single mutant; in the double mutant, however, after UV irradiation chromosomal DNA was degraded to the same extent as in the JK57 mutant. The number of transformants per unit of radioactive donor DNA taken up by JK57 recipient cells was approximately 10-fold smaller than in the wild type. Presynaptically, the fate of donor DNA in the adenosine 5'-triphosphate-dependent deoxyribonuclease-deficient mutants was not different from that in the wild type. In contrast to TD24 and the TD2457 double mutant, in the JK57 mutant, recombinant-type activities (molecules carrying both the donor and recipient markers) were formed almost as well as in the wild type. After integration into the JK57 recipient genome, the rate of replication of the donor marker was equal to that of the recipient marker during a number of generations, which suggests that the donor DNA is normally integrated into the JK57 chromosome. It is suggested that transformed JK57 cells pass with a high frequency into a type of cells that can replicate their chromosomes many times but have lost the ability to form visible colonies after plating.

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Section: Discussionmentioning

confidence: 99%

Effect of adenosine 5'-triphosphate-dependent deoxyribonuclease deficiency on properties and transformation of Haemophilus influenzae strains

Kooistra¹,

Venema²

1976

J Bacteriol

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“…Ohi et a/. [25] have reported a value of 260000 for this enzyme, estimated from sedimentation data in sucrose gradient. Molecular weight estimates for the purified ATP-dependent DNAases of two other bacterial species are the following: H. influenzae, 270000 (sucrose gradient centrifugation) [lo] and 290000 (dodecylsulfate-polyacrylamide gel electrophoresis) [26] ; E. coli 350000 (sedimentation rate) [27], 250 000 (glycerol gradient centrifugation), 270 000 (dodecylsulfate-polyacrylamide gel electrophoresis) [9].…”

Section: Discussionmentioning

confidence: 99%

Isolation, Subunit Structure and Properties of the ATP‐Dependent Deoxyribonuclease of Bacillus subtilis

Doly

Anagnostopoulos

1976

European Journal of Biochemistry

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A procedure was developed for the purification of the ATP‐dependent deoxyribonuclease of Bacillus subtilis 168. It comprises ammonium sulphate fractionation, Sephadex gel filtration, DFAE‐cellulose chromatography and gel electrophoresis on a discontinuous polyacrylamide gradient. The enzyme has been obtained in a homogeneous state. Its molecular weight was estimated to be 270000 by disc electrophoresis. Dodecylsulfate‐polyacrylamide gel electrophoresis showed the presence of five nonidentical subunits of the following molecular weights: 81 000, 70 000, 62000, 52 500 and 42 500. These values give 308 000 as the molecular weight of the native enzyme. The pH optimum of the purified enzyme is 9.6. The optimal concentrations of Mg2+ and ATP for exonuclease activity on native B. subtilis DNA were determined. ATP‐requirement for hydrolysis of single‐stranded DNA is less stringent. The enzyme also possesses high DNA‐dependent ATPase activity. The purification procedure was applied to extracts of a mutant devoid of activity for this enzyme (strain GSY 1290). A protein was isolated which is very similar to the active DNAase as regards electrophoretic mobility, reaction with specific antisera and size of four of the subunits. One subunit is missing (Mr 70 000) and is replaced by a smaller polypeptide (Mr 56 500). The latter results suggest that the mutant is affected in the genetic locus coding for the 70 000‐Mr subunit.

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DNA-Dependent ATPases and Viceversa

Whitehead

Palitti²,

Cerio-Ventura³

et al. 1979

Macromolecules in the Functioning Cell

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Biological Sciences: Non-specific ‘pairing’ of DNA molecules by recombination enzyme of Bacillus subtilis

Cited by 8 publications

References 21 publications

Effect of adenosine 5'-triphosphate-dependent deoxyribonuclease deficiency on properties and transformation of Haemophilus influenzae strains

Effect of adenosine 5'-triphosphate-dependent deoxyribonuclease deficiency on properties and transformation of Haemophilus influenzae strains

Isolation, Subunit Structure and Properties of the ATP‐Dependent Deoxyribonuclease of Bacillus subtilis

DNA-Dependent ATPases and Viceversa

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