Deoxyribonuclease Activity Associated with Adenovirus 5 and 7

Cajean-Feroldi, Chantal; Chardonnet, Y; Chantepie-Auray, Jacqueline

doi:10.1111/j.1432-1033.1977.tb11412.x

Cited by 6 publications

(3 citation statements)

References 22 publications

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“…Recently these observations have been confirmed by Marusyk et al [3] and by Cajean-Feroldi et al [4], who reported on an endonuclease in association with pentons of adenovirus types 2, 3, 5, 7, 9, 12, 15 and 16. Under the conditions used by Marusyk et al [3] the endonucleolytic activity caused predominantly single-strand scissions in the DNA substrate.…”

supporting

confidence: 76%

“…In previous work an endonuclease specific for double-stranded DNA has been described in association with the penton subunit of adenovirus type 2 [l], in extracts of KB cells infected with adenovirus types 2 and 12 and in association with purified preparations of adenovirus [2]. Recently these observations have been confirmed by Marusyk et al [3] and by Cajean-Feroldi et al [4], who reported on an endonuclease in association with pentons of adenovirus types 2, 3, 5, 7, 9, 12, 15 and 16. Under the conditions used by Marusyk et al [3] the endonucleolytic activity caused predominantly single-strand scissions in the DNA substrate.…”

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confidence: 70%

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Purification of an Endonuclease from Adenovirus‐Infected KB Cells

Reif

Winterhoff

Lundholm

et al. 1977

European Journal of Biochemistry

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This report describes the purification of an endonuclease from extracts of adenovirus-type-2-infected KB cells. Endonuclease activity can also be detected in extracts of uninfected KB cells and the enzyme activities from extracts of uninfected and adenovirus-infected cells are very similar, if not identical. The enzyme has its maximal activity at pH 4.0. The enzyme found in uninfected and adenovirus-infected cells is, however, strikingly different from an endonuclease isolated from calf serum. Hence, the endonuclease described is probably not a contaminant derived from the medium in which the KB cells were propagated.The endonuclease in crude extracts from uninfected or adenovirus-infected KB cells can be activated or its activity enhanced by treatment of the extracts with proteolytic enzymes, like pronase or trypsin. Evidence has been presented suggesting that this activation is due to proteolytic cleavage of an inhibitor present in crude extracts of uninfected and adenovirus-type-2-infected KB cells.A second endonuclease has been found in extracts of infected and uninfected cells with optimal activity at pH 7.2 and this endonuclease can be separated from the one with a pH optimum at 4.0.In previous work an endonuclease specific for double-stranded DNA has been described in association with the penton subunit of adenovirus type 2 [l], in extracts of KB cells infected with adenovirus types 2 and 12 and in association with purified

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supporting

confidence: 76%

mentioning

confidence: 70%

Purification of an Endonuclease from Adenovirus‐Infected KB Cells

Reif

Winterhoff

Lundholm

et al. 1977

European Journal of Biochemistry

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“…In addition to these endonuclease activities probably coded for by the host genome, an endonuclease specific for double-stranded DNA has been described in association with the penton subunit of Ad 2 (4,5). Marusyk et Abbreviation used: Ad, adenovirus, TCA, trichloroacetic acid; d*G denotes d32P G. C) Information Retrieval Limited 1 Falconberg Court London Wl V 5FG England al (6) and Cajean-Feroldi et al (7) confirmed and extended the observations that the pentons of adenovirus types 2, 3, 5, 7, 9, 12, 15 and 16 were associated with an endonuclease. Under the conditions used by Marusyk et al (6), the penton-associated endonuclease caused predominantly single-strand scissions in the DNA substrate.…”

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confidence: 99%

Specificity and mode of cleavage of the pH 4.0 endonuclease from adenovirus type 2-infected KB cells

et al. 1979

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Adenovirus type 2 or X DNA was digested with the pH 4.0 endonuclease, purified from adenovirus 2-infected KB cells. The enzyme produces a limit digest of approximate size in the range of 140-210 base pairs long. The termini of the DNA fragments generated by the endonuclease digestion had 3'-P and 5'-OH groups. The 3' and 5' end groups of the products were analyzed. Our data indicate that 3' end group was a purine (68-76%), dA occuring about twice the frequency of dG. The 5' end group was either dG or dC with equal frequency. Data obtained by treatment of the 5' labeled endonuclease product of X DNA with single-strand specific S1 nuclease from Asperigillus oryzae or exonuclease VII from Escherichia coli indicated that the majority of the products had a short 5' protruding ends. The mode of cleavage of this endonuclease seems to be through initial formation of several single-strand breaks with some base specificity. If these breaks are at close proximity on opposite strands, double-stranded fragments with protruding ends are generated. INTRODUCTIONRecently, Reif et al (1,2) reported the purification and identification of two endonucleases from adenovirus (Ad) type 2 infected KB cells. These activities were also found to be present in uninfected human KB cells. These endonuclease activities are distinguished by their pH optima at pH 4.0 and pH 7.2. Tsuruo et al (3) found an endonuclease present in both uninfected and Ad 2-infected KB cells which had a pH optimum of 8.8 in Tris-HCl buffer. In addition to these endonuclease activities probably coded for by the host genome, an endonuclease specific for double-stranded DNA has been described in association with the penton subunit of Ad 2 (4,5). Marusyk et

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Structural and Nonstructural Adenovirus Proteins

Pettersson

1984

The Adenoviruses

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Deoxyribonuclease Activity Associated with Adenovirus 5 and 7

Cited by 6 publications

References 22 publications

Purification of an Endonuclease from Adenovirus‐Infected KB Cells

Purification of an Endonuclease from Adenovirus‐Infected KB Cells

Specificity and mode of cleavage of the pH 4.0 endonuclease from adenovirus type 2-infected KB cells

Structural and Nonstructural Adenovirus Proteins

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