The ultraviolet endonuclease of bacteriophage T4. Further characterization.

Minton, Kenneth W.; Durphy, Michael; Taylor, Russell E.; Friedberg, Errol C.

doi:10.1016/s0021-9258(19)41564-0

Cited by 61 publications

(4 citation statements)

References 25 publications

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“…polynucleotide ligase both in vivo and in vitro (Seeberg, Rupp, and Braun, manuscript in preparation). Similar observations have recently been reported by Minton et al (1975) in the T4 phage induced correndonuclease II. Such evidence supports the mechanism of endonuclease action in generating S'-phosphoryl termini.…”

Section: Discussionsupporting

confidence: 91%

Enzymic repair of DNA: sites of hydrolysis by the Escherichia coli endonuclease specific for pyrimidine dimers (correndonuclease II)

Braun¹,

Radman²,

Grossman³

1976

Biochemistry

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10-2 M Tris (pH 8)-10-2 M NaCl-10-2 M EDTA: EDTA, ethylencdiaminetetraacetic acid; uv, ultraviolet; BAP, bacterial alkaline phosphatase: DEAE. diethylaminoethyl; KA buffer. 0.05 M potassium phosphate (pH 7.5)-0.005 M 2-mercaptoethanol-0.001 M EDTA; Tris. tris(hydroxymethyl)aminomethane. Correndonuclease 11 refers to an endonuclease eventuating in the excision repair of intrastrand pyrimidine dimers (see review by Grossman et al. (1975)).

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Section: Discussionsupporting

confidence: 91%

Enzymic repair of DNA: sites of hydrolysis by the Escherichia coli endonuclease specific for pyrimidine dimers (correndonuclease II)

Braun¹,

Radman²,

Grossman³

1976

Biochemistry

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“…monomer-dimer equilibrium in solution. Our results and those of Minton et al (1975) demonstrate that under low-salt conditions the monomer state is highly favored. Under (O); pGX2608-<fenV-Leu-59, .…”

Section: Discussionsupporting

confidence: 74%

Mutations in endonuclease V that affect both protein-protein association and target site location

Nickell¹,

Lloyd²

1991

Biochemistry

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A general mechanism by which proteins locate their target sites within large domains of DNA is a one-dimensional facilitated diffusion process in which the protein scans DNA in a nonspecifically bound state. An electrostatic contribution to this type of mechanism has been previously established. This study was designed to question whether other characteristics of a protein's structure might contribute to the scanning mechanism of target site location. In this regard, T4 endonuclease V was shown to establish an ionic strength dependent monomer-dimer equilibrium in solution. A protein dimer interaction site was postulated to exist along a putative alpha-helix containing amino acid residues 54-62. The conservative substitutions of Phe-60----Leu-60 and Phe-59, Phe-60----Leu-59, Leu-60 resulted in mutant enzymes which remained in the monomeric state independent of the ionic strength of the solution. The target site location mechanism of these mutants has also been altered. Under conditions where wild-type endonuclease V processively scans nontarget DNA, the target location mechanism of the monomeric mutant proteins was shifted toward a less processive search. This decrease in the processivity of the mutants was especially surprising because the nontarget DNA binding affinity was found to be significantly increased. Thus, an additional component of the endonuclease V DNA scanning mechanism appears to be the formation of a stable endonuclease V dimer complex.

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“…This enzyme was originally identified by the observation that E. coli infected with bacteriophage T4 are able to release nucleotides containing pyrimidine dimers from UV-irradiated cells. This activity is the result of the bacteriophage T4 denV gene product, T4-endo V. − , T4-endo V was later characterized thoroughly and shown to cleave the N-glycosyl bond of 5‘-pyrimidines at dimers of adjacent pyrimidines with subsequent AP endonuclease activity to give phosphodiester bond cleavage between the dimerized pyrimidines. − ,− Sequencing and overexpression of this enzyme have facilitated its characterization . Enzymes with similar activity have also been isolated from Micrococcus luteus ( M. luteus UV-endonuclease) − and S. cerevisiae .…”

Section: E Pyrimidine Dimer Glycosylasesmentioning

confidence: 99%

Chemistry of Glycosylases and Endonucleases Involved in Base-Excision Repair

1998

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ContentsI. Introduction 1221 II. Types of Base-Excision Repair Glycosylases 1223 A. Uracil-DNA Glycosylase (UDG) 1223 B. Mismatch-Specific Thymine-DNA Glycosylase (TDG) and Related Double-Strand Specific Uracil DNA Glycosylase (dsUDG) 1226 C. Alkylated Base Removal 1227 D. Endonuclease III and Related Enzymes 1229 E. Pyrimidine Dimer Glycosylases 1230 F. The FPG Protein (Fapy Glycosylase or MutM) 1231

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The ultraviolet endonuclease of bacteriophage T4. Further characterization.

Cited by 61 publications

References 25 publications

Enzymic repair of DNA: sites of hydrolysis by the Escherichia coli endonuclease specific for pyrimidine dimers (correndonuclease II)

Enzymic repair of DNA: sites of hydrolysis by the Escherichia coli endonuclease specific for pyrimidine dimers (correndonuclease II)

Mutations in endonuclease V that affect both protein-protein association and target site location

Chemistry of Glycosylases and Endonucleases Involved in Base-Excision Repair

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