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Modulation of hyperthermophilic DNA polymerase activity by archaeal chromatin proteins
- Source :
- The Journal of biological chemistry. 279(1)
- Publication Year :
- 2003
-
Abstract
- Sulfolobus synthesizes a large quantity of highly conserved 7-kDa DNA-binding proteins suspected to be involved in chromosomal organization. The effect of the 7-kDa proteins on the polymerization and 3'-5' exonuclease activities of a family B DNA polymerase (polB1) from the hyperthermophilic archaeon Sulfolobus solfataricus was investigated. polB1 degraded both single-stranded DNA and double-stranded DNA at similar rates in vitro at temperatures of physiological relevance. The 7-kDa proteins were capable of significantly inhibiting the excision and enhancing the extension of matched template primers by the polymerase. However, the proteins did not protect single-stranded DNA from cleavage by polB1. In addition, the 7-kDa proteins did not affect the proofreading ability of polB1 and were not inhibitory to the excision of mismatched primers by the polymerase. The dNTP concentrations required for the effective inhibition of the 3'-5' exonuclease activity of polB1 were lowered from approximately 1 mm in the absence of the 7-kDa proteins to approximately 50 microm in the presence of the proteins at 65 degrees C. Our data suggest that the 7-kDa chromatin proteins serve to modulate the extension and excision activities of the hyperthermophilic DNA polymerase, reducing the cost of proofreading by the enzyme at high temperature.
- Subjects :
- Exonucleases
DNA polymerase
DNA polymerase II
Archaeal Proteins
ved/biology.organism_classification_rank.species
Molecular Sequence Data
DNA-Directed DNA Polymerase
Biochemistry
Sulfolobus
chemistry.chemical_compound
Molecular Biology
Polymerase
Klenow fragment
DNA Primers
DNA clamp
biology
Base Sequence
ved/biology
Sulfolobus solfataricus
DNA replication
Cell Biology
Templates, Genetic
Molecular biology
Chromatin
Molecular Weight
Kinetics
chemistry
biology.protein
Thermodynamics
DNA
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 279
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- The Journal of biological chemistry
- Accession number :
- edsair.doi.dedup.....c4d400ecbefc3ccb3c5f6398ad9fbcc5