Catalytic and binding mutants of the junction-resolving enzyme endonuclease I of bacteriophage t7: role of acidic residues.

@article{Parkinson1999CatalyticAB,
  title={Catalytic and binding mutants of the junction-resolving enzyme endonuclease I of bacteriophage t7: role of acidic residues.},
  author={Matthew J. Parkinson and J R P{\"o}hler and David M. J. Lilley},
  journal={Nucleic acids research},
  year={1999},
  volume={27 2},
  pages={682-9}
}
Endonuclease I is a 149 amino acid protein of bacteriophage T7 that is a Holliday junction-resolving enzyme, i.e. a four-way junction-selective nuclease. We have performed a systematic mutagenesis study of this protein, whereby all acidic amino acids have been individually replaced by other residues, mainly alanine. Out of 21 acidic residues, five (Glu20, Glu35, Glu65, Asp55 and Asp74) are essential. Replacement of these residues by other amino acids leads to a protein that is inactive in the… CONTINUE READING

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We have performed a systematic mutagenesis study of this protein , whereby all acidic amino acids have been individually replaced by other residues , mainly alanine .
We have performed a systematic mutagenesis study of this protein , whereby all acidic amino acids have been individually replaced by other residues , mainly alanine .
We have performed a systematic mutagenesis study of this protein , whereby all acidic amino acids have been individually replaced by other residues , mainly alanine .
We have performed a systematic mutagenesis study of this protein , whereby all acidic amino acids have been individually replaced by other residues , mainly alanine .
We have performed a systematic mutagenesis study of this protein , whereby all acidic amino acids have been individually replaced by other residues , mainly alanine .
Amino AcidsChemical structure ofAlanine
We have performed a systematic mutagenesis study of this protein , whereby all acidic amino acids have been individually replaced by other residues , mainly alanine .
We have also constructed a mutant of endonuclease I that lacks nine amino acids ( six of which are arginine or lysine ) at the C - terminus .
We have also constructed a mutant of endonuclease I that lacks nine amino acids ( six of which are arginine or lysine ) at the C - terminus .
ArginineNo subtypeLysine
We have also constructed a mutant of endonuclease I that lacks nine amino acids ( six of which are arginine or lysine ) at the C - terminus .
LysineNo subtypeArginine
We have also constructed a mutant of endonuclease I that lacks nine amino acids ( six of which are arginine or lysine ) at the C - terminus .
Endonuclease I is a 149 amino acid protein of bacteriophage T7 that is a Holliday junction - resolving enzyme , i.e. a four - way junction - selective nuclease .
We have also constructed a mutant of endonuclease I that lacks nine amino acids ( six of which are arginine or lysine ) at the C - terminus .
We have also constructed a mutant of endonuclease I that lacks nine amino acids ( six of which are arginine or lysine ) at the C - terminus .
Endonuclease I is a 149 amino acid protein of bacteriophage T7 that is a Holliday junction - resolving enzyme , i.e. a four - way junction - selective nuclease .
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