Structure-function studies of the T4 endonuclease V repair enzyme

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

Published data on the structure and mechanism of endonuclease V from bacteriophage T4 are reviewed with the objective of developing a working mechanistic model of this enzyme. Endonuclease V is an interesting and important candidate to be the first DNA-repair enzyme to have its structure determined by crystallography, and a more detailed model of the reaction process is needed to mechanistically interpret such a structure. Such a model should be sufficiently detailed to support future investigations of structure/function relationships between the enzyme and the DNA damage repair pathway it initiates, as probed by site-directed mutagenesis techniques and other methods. The early literature is presented in an historical perspective, followed by a description of prior models and biochemical investigations. The biochemical phenotypes of mutants in the enzyme structural gene are discussed. The results of computer analyses aimed at structural interpretations of the protein sequence are given, together with a brief discussion of the strengths and weaknesses of such experiments.

Original languageEnglish (US)
Pages (from-to)49-65
Number of pages17
JournalMutation Research-DNA Repair
Volume218
Issue number2
DOIs
StatePublished - 1989
Externally publishedYes

Fingerprint

Repair
Deoxyribonuclease (Pyrimidine Dimer)
Enzymes
DNA Repair Enzymes
Crystallography
Site-Directed Mutagenesis
DNA Repair
Mutagenesis
DNA Damage
Phenotype
Genes
phage T4 endonuclease V
DNA
Proteins
Experiments

Keywords

  • Endonuclease V, T4
  • Enzyme function
  • Enzyme mechanism
  • Enzyme structure
  • Pyrimidine dimer
  • T4 endonuclease V

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology
  • Toxicology
  • Medicine(all)

Cite this

Structure-function studies of the T4 endonuclease V repair enzyme. / Dodson, M. L.; Lloyd, Robert (Stephen).

In: Mutation Research-DNA Repair, Vol. 218, No. 2, 1989, p. 49-65.

Research output: Contribution to journalArticle

@article{5b2f2072a9154c829e4667f1e1383129,
title = "Structure-function studies of the T4 endonuclease V repair enzyme",
abstract = "Published data on the structure and mechanism of endonuclease V from bacteriophage T4 are reviewed with the objective of developing a working mechanistic model of this enzyme. Endonuclease V is an interesting and important candidate to be the first DNA-repair enzyme to have its structure determined by crystallography, and a more detailed model of the reaction process is needed to mechanistically interpret such a structure. Such a model should be sufficiently detailed to support future investigations of structure/function relationships between the enzyme and the DNA damage repair pathway it initiates, as probed by site-directed mutagenesis techniques and other methods. The early literature is presented in an historical perspective, followed by a description of prior models and biochemical investigations. The biochemical phenotypes of mutants in the enzyme structural gene are discussed. The results of computer analyses aimed at structural interpretations of the protein sequence are given, together with a brief discussion of the strengths and weaknesses of such experiments.",
keywords = "Endonuclease V, T4, Enzyme function, Enzyme mechanism, Enzyme structure, Pyrimidine dimer, T4 endonuclease V",
author = "Dodson, {M. L.} and Lloyd, {Robert (Stephen)}",
year = "1989",
doi = "10.1016/0921-8777(89)90011-6",
language = "English (US)",
volume = "218",
pages = "49--65",
journal = "Mutation Research - DNA Repair",
issn = "0921-8777",
publisher = "Elsevier BV",
number = "2",

}

TY - JOUR

T1 - Structure-function studies of the T4 endonuclease V repair enzyme

AU - Dodson, M. L.

AU - Lloyd, Robert (Stephen)

PY - 1989

Y1 - 1989

N2 - Published data on the structure and mechanism of endonuclease V from bacteriophage T4 are reviewed with the objective of developing a working mechanistic model of this enzyme. Endonuclease V is an interesting and important candidate to be the first DNA-repair enzyme to have its structure determined by crystallography, and a more detailed model of the reaction process is needed to mechanistically interpret such a structure. Such a model should be sufficiently detailed to support future investigations of structure/function relationships between the enzyme and the DNA damage repair pathway it initiates, as probed by site-directed mutagenesis techniques and other methods. The early literature is presented in an historical perspective, followed by a description of prior models and biochemical investigations. The biochemical phenotypes of mutants in the enzyme structural gene are discussed. The results of computer analyses aimed at structural interpretations of the protein sequence are given, together with a brief discussion of the strengths and weaknesses of such experiments.

AB - Published data on the structure and mechanism of endonuclease V from bacteriophage T4 are reviewed with the objective of developing a working mechanistic model of this enzyme. Endonuclease V is an interesting and important candidate to be the first DNA-repair enzyme to have its structure determined by crystallography, and a more detailed model of the reaction process is needed to mechanistically interpret such a structure. Such a model should be sufficiently detailed to support future investigations of structure/function relationships between the enzyme and the DNA damage repair pathway it initiates, as probed by site-directed mutagenesis techniques and other methods. The early literature is presented in an historical perspective, followed by a description of prior models and biochemical investigations. The biochemical phenotypes of mutants in the enzyme structural gene are discussed. The results of computer analyses aimed at structural interpretations of the protein sequence are given, together with a brief discussion of the strengths and weaknesses of such experiments.

KW - Endonuclease V, T4

KW - Enzyme function

KW - Enzyme mechanism

KW - Enzyme structure

KW - Pyrimidine dimer

KW - T4 endonuclease V

UR - http://www.scopus.com/inward/record.url?scp=0024452308&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024452308&partnerID=8YFLogxK

U2 - 10.1016/0921-8777(89)90011-6

DO - 10.1016/0921-8777(89)90011-6

M3 - Article

VL - 218

SP - 49

EP - 65

JO - Mutation Research - DNA Repair

JF - Mutation Research - DNA Repair

SN - 0921-8777

IS - 2

ER -