Researchers Characterize PrimPol, a Novel Human DNA Polymerase
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By LabMedica International staff writers Posted on 19 Nov 2013 |
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PrimPol, a novel enzyme cloned in human cells, has been shown to initiate DNA chains with deoxynucleotides unlike regular primases, which exclusively use ribonucleotides.
Investigators at the biotechnology company SYGNIS AG (Madrid, Spain; and Heidelberg, Germany) in collaboration with researchers at the Spanish National Research Council (Madrid) recently isolated and characterized PrimPol.
They reported in the October 24, 2013, online edition of the journal Molecular Cell that PrimPol functioned as both DNA primase and DNA polymerase, and demonstrated high tolerance to damaged DNA. The primase function of PrimPol allowed it to begin reading and copying DNA without the need for random ribonucleotide primers, as required by all other commercially available polymerases. The use of random primers can bias sequencing and amplification results. The polymerase function of PrimPol displayed high specific activity, being extremely efficient when copying DNA strands with different lesions, such as abasic sites or 8-oxoguanine.
Subcellular fractionation and immunodetection studies showed that PrimPol could be found in both nuclear and mitochondrial DNA compartments. Its activity was detectable in mitochondrial lysates from human and mouse cells but was absent from mitochondria derived from mice that had been genetically engineered to lack the PRIMPOL gene. PRIMPOL gene silencing or ablation in human and mouse cells impaired mitochondrial DNA replication.
Senior author Dr. Luis Blanco, research professor at the Spanish National Research Council, said, "I am convinced that this fantastic enzyme will open numerous novel applications in the field of molecular biology, some of them we can only hint at this moment given the highly innovative potential of its key features."
SYGNIS AG is currently developing a new thermostable version of the enzyme that is expected to make an important contribution to the DNA amplification and sequencing field.
Related Links:
SYGNIS AG
Spanish National Research Council
Investigators at the biotechnology company SYGNIS AG (Madrid, Spain; and Heidelberg, Germany) in collaboration with researchers at the Spanish National Research Council (Madrid) recently isolated and characterized PrimPol.
They reported in the October 24, 2013, online edition of the journal Molecular Cell that PrimPol functioned as both DNA primase and DNA polymerase, and demonstrated high tolerance to damaged DNA. The primase function of PrimPol allowed it to begin reading and copying DNA without the need for random ribonucleotide primers, as required by all other commercially available polymerases. The use of random primers can bias sequencing and amplification results. The polymerase function of PrimPol displayed high specific activity, being extremely efficient when copying DNA strands with different lesions, such as abasic sites or 8-oxoguanine.
Subcellular fractionation and immunodetection studies showed that PrimPol could be found in both nuclear and mitochondrial DNA compartments. Its activity was detectable in mitochondrial lysates from human and mouse cells but was absent from mitochondria derived from mice that had been genetically engineered to lack the PRIMPOL gene. PRIMPOL gene silencing or ablation in human and mouse cells impaired mitochondrial DNA replication.
Senior author Dr. Luis Blanco, research professor at the Spanish National Research Council, said, "I am convinced that this fantastic enzyme will open numerous novel applications in the field of molecular biology, some of them we can only hint at this moment given the highly innovative potential of its key features."
SYGNIS AG is currently developing a new thermostable version of the enzyme that is expected to make an important contribution to the DNA amplification and sequencing field.
Related Links:
SYGNIS AG
Spanish National Research Council
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