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Two Holliday junction resolving enzymes in Sulfolobus solfataricus.
- Source :
-
Journal of molecular biology [J Mol Biol] 2000 Apr 07; Vol. 297 (4), pp. 923-32. - Publication Year :
- 2000
-
Abstract
- Holliday junction resolving enzymes bind specifically to four-way DNA junctions created by the process of homologous recombination, cleaving them to yield recombinant duplex DNA products. Homologous recombination is known to occur in the third domain of life, the archaea, and may constitute a simplified model for the corresponding eucaryal pathway, but has not been well characterised. Identification of a gene encoding an archaeal Holliday junction resolving enzyme, Hjc, has recently been reported in the euryarchaea, and an activity has been observed in the hyperthermophilic crenarchaeote Sulfolobus solfataricus. Here we report the identification, heterologous expression and characterisation of the Hjc protein from Sulfolobus. We demonstrate that Sulfolobus has two distinct junction resolving enzymes, Hjc and Hje, with differing substrate specificities.<br /> (Copyright 2000 Academic Press.)
- Subjects :
- Amino Acid Sequence
Archaeal Proteins immunology
Base Sequence
Cloning, Molecular
DNA chemistry
DNA genetics
DNA metabolism
DNA-Binding Proteins chemistry
DNA-Binding Proteins genetics
DNA-Binding Proteins immunology
DNA-Binding Proteins metabolism
Endodeoxyribonucleases chemistry
Endodeoxyribonucleases genetics
Endodeoxyribonucleases immunology
Genes, Archaeal genetics
Holliday Junction Resolvases
Magnesium pharmacology
Molecular Sequence Data
Nucleic Acid Conformation
Open Reading Frames genetics
Protein Binding drug effects
Recombinant Proteins chemistry
Recombinant Proteins immunology
Recombinant Proteins isolation & purification
Recombinant Proteins metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Substrate Specificity
Thermodynamics
Archaeal Proteins metabolism
Endodeoxyribonucleases metabolism
Recombination, Genetic genetics
Sulfolobus enzymology
Sulfolobus genetics
Subjects
Details
- Language :
- English
- ISSN :
- 0022-2836
- Volume :
- 297
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Journal of molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 10736227
- Full Text :
- https://doi.org/10.1006/jmbi.2000.3624