The Escherichia coli B restriction endonuclease

Roulland-Dussoix, Daisy; Boyer, Herbert W.

doi:10.1016/0005-2787(69)90618-2

Cited by 81 publications

(30 citation statements)

References 20 publications

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“…Escherichia coli strain HB129 was derived from an endonuclease I deficient E. coli 1100 (10,11). MB100 was derived from HB129 by transformation with the plasmid pMBl (molecular weight 5.5 X 106 daltons), which is similar to colicin El (col El) (12) except that it carries an additional 1.3 X 106 dalton piece of DNA containing the EcoRI restriction and modification genes (M. C. Betlach, unpublished observation).…”

Section: Methodsmentioning

confidence: 99%

Specificity of substrate recognition by the EcoRI restriction endonuclease.

Polisky¹,

Greene²,

Garfin³

et al. 1975

Proc. Natl. Acad. Sci. U.S.A.

273

133

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Section: Methodsmentioning

confidence: 99%

Specificity of substrate recognition by the EcoRI restriction endonuclease.

Polisky¹,

Greene²,

Garfin³

et al. 1975

Proc. Natl. Acad. Sci. U.S.A.

273

133

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“…Arber) (2), HB129 (obtained from H. W. Boyer) (33), and BZ216 (obtained from T. A. Bickle) are the rA+ mA+, rB+ mB', and rD' mD' derivatives of E. coli K-12, respectively.…”

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confidence: 99%

Nucleotide sequence of the gene (ard) encoding the antirestriction protein of plasmid colIb-P9

Delver¹,

Kotova²,

Zavilgelsky³

et al. 1991

J Bacteriol

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The IncIl plasmid ColIb-P9 was found to encode an antirestriction function. The relevant gene, ard (alleviation of restriction of DNA), maps about 5 kb from the origin of transfer, in the region transferred early during bacterial conjugation. Ard inhibits both restriction and modification by each of the four type I systems of Escherichia coli tested, but it had no effect on restriction by either EcoRI, a type II system, or EcoPl, a type III system. The nucleotide sequence of the ColIb ard gene was determined; the predicted molecular weight of the Ard polypeptide is 19,193. The proposed polypeptide chain contains an excess of 25 negatively charged amino acids, suggesting that its overall character is very acidic. Deletion analysis of the gene revealed that the Ard protein contained a distinct functional domain located in the COOH-terminal half of the polypeptide. We suggest that the biological role of the ColIb Ard protein is associated with overcoming host-controlled restriction during bacterial conjugation.

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“…The restriction and modification enzymes of several host specificities (1)(2)(3)(4)(5)(6)(7), including the endonuclease and methylase of the host-specificity (RI) controlled by the fi+ R-factor (Yoshimori, Roulland-Dussoix, Aldridge & Boyer; Yoshimori, Roulland-Dussoix, Goodman & Boyer, to be published) have been characterized. The restriction endonuclease of a given host specificity interacts with a specific sequence of DNA base-pairs and produces a double-strand break in the molecule (1)(2)(3)(4)(5)(6), while the modification methylase methylates a base in each strand of this sequence (refs.…”

mentioning

confidence: 99%

“…The restriction endonuclease of a given host specificity interacts with a specific sequence of DNA base-pairs and produces a double-strand break in the molecule (1)(2)(3)(4)(5)(6), while the modification methylase methylates a base in each strand of this sequence (refs. 3 and 7; Yoshimori, Roulland-Dussoix, Goodman & Boyer, to be published).…”

mentioning

confidence: 99%

DNA Nucleotide Sequence Restricted by the RI Endonuclease

Hedgpeth

Goodman

Boyer

1972

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

318

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The sequence of DNA base pairs adjacent to the phosphodiester bonds cleaved by the RI restriction endonuclease in unmodified DNA from coliphage X has been determined. The 5'-terminal nucleotide labeled with 32p and oligonucleotides up to the heptamer were analyzed from a pancreatic DNase digest. The following sequence of nucleotides adjacent to the RI break made in X DNA was deduced from these data and from the 3'-dinucleotide sequence and nearest-neighbor analysis obtained from repair synthesis with the DNA polymerase of Rous sarcoma virusThe RI endonuclease cleavage of the phosphodiester bonds (indicated by arrows) generates 5'-phosphoryls and short cohesive termini of four nucleotides, pApApTpT. The most striking feature of the sequence is its symmetry.The restriction and modification enzymes of several host specificities (1-7), including the endonuclease and methylase of the host-specificity (RI) controlled by the fi+ R-factor (Yoshimori, Roulland-Dussoix, Aldridge & Boyer; Yoshimori, Roulland-Dussoix, Goodman & Boyer, to be published) have been characterized. The restriction endonuclease of a given host specificity interacts with a specific sequence of DNA base-pairs and produces a double-strand break in the molecule (1-6), while the modification methylase methylates a base in each strand of this sequence (refs. 3 and 7; Yoshimori, Roulland-Dussoix, Goodman & Boyer, to be published). Methylation of a base in either strand is sufficient to prevent the endonuclease from attacking the sequence (3). Therefore, in molecular terms, a given DNA restriction and modification host-specificity can be defined by the sequence of base pairs recognized by the restriction endonuclease and modification methylase. In this paper, we present an analysis of the sequence of base pairs adjacent to the phosphodiester bond cleavages made in bacteriophage X DNA by the RI restriction endonuclease. MATERIALS AND METHODSEnzyme. The RI restriction endonuclease, purified as will be described by Yoshimori, Roulland-Dussiox, Aldridge, and Boyer (to be published), was free of detectable nonspecific exo-or endonuclease activities and migrated as one band in native or Na dodecyl S04-polyacrylamide gels. Purified RNAdirected DNA polymerase of Rous Sarcoma virus, free of detectable exo-or endonucleolytic activities (8,9), was a generous gift from Dr. A. J. Faras. Polynucleotide kinase (10) was purified as described elsewhere. Escherichia coli alkaline phosphatase rechromatographed as described elsewhere (11), pancreatic DNase, micrococcal nuclease, venom phosphodiesterase, and spleen phosphodiesterase were obtained from Worthington Biochemical Co.Phage X DNA. A X (CI857SUSS7) lysogen of E. coli 1100 was used as a source of X phage. Tryptone broth cultures of lysogens (2 X 108 cell per ml) were heated to 420 for 0.5 hr (isotope was added here for labeled DNA) and incubated at 370 for 3 hr. The cells were collected by low-speed centrifugation and resuspended in 5-10 ml of 50 mM Tris-HCl (pH 7.5)-10 mM MgCl2. 0.5 ml of CHC13 was added and ...

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The Escherichia coli B restriction endonuclease

Cited by 81 publications

References 20 publications

Specificity of substrate recognition by the EcoRI restriction endonuclease.

Specificity of substrate recognition by the EcoRI restriction endonuclease.

Nucleotide sequence of the gene (ard) encoding the antirestriction protein of plasmid colIb-P9

DNA Nucleotide Sequence Restricted by the RI Endonuclease

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