Dna Polymerase in a sentence

DNA polymerase and RNA polymerase are used to assemble DNA and RNA molecules, respectively, by copying a DNA or RNA template strand using base-pairing interactions.

The DNA polymerase isolated from T. aquaticus is stable at high temperatures remaining active even after DNA denaturation, thus obviating the need to add new DNA polymerase after each cycle.

Via a thorough study, the Eukaryotic DNA Polymerase report discovers the foremost approaches of speculation for the Eukaryotic DNA Polymerase market.

Once the polymerase reaches the end of the template or detects double-stranded DNA, the sliding clamp undergoes a conformational change that releases the DNA polymerase.

The RNA fragments are then removed by DNA polymerase I for prokaryotes or DNA polymerase δ for eukaryotes (different mechanisms are used in eukaryotes and prokaryotes ) and new deoxyribonucleotides are added to fill the gaps where the RNA was present.

Directionality has consequences in DNA synthesis, because DNA polymerase can synthesize DNA in only one direction by adding nucleotides to the 3' end of a DNA strand.

Very low dNTP concentration inhibits DNA synthesis and DNA repair and is lethal to the cell, while an abnormal ratio of dNTPs is mutagenic due to the increased likelihood of the DNA polymerase incorporating the wrong dNTP during DNA synthesis.

RNase removes the primer RNA fragments, and a low processivity DNA polymerase distinct from the replicative polymerase enters to fill the gaps.

More RNA primers attach further on the DNA strand and DNA polymerase comes along and continues to make a new DNA strand.

The insertion sites of DNA transposons may be identified by short direct repeats (created by the staggered cut in the target DNA and filling in by DNA polymerase) followed by a series of inverted repeats important for the TE excision by transposase.

The RNA strands are replaced with newly synthesized DNA, but DNA polymerase can only "backfill" deoxyribonucleotides if there is already DNA "upstream" from (i.

This step cuts out the DNA transposon, which is then ligated into a new target site; the process involves activity of a DNA polymerase that fills in gaps and of a DNA ligase that closes the sugar-phosphate backbone.

At the chromosome terminal, however, there is no nucleotide sequence in the 5' direction (and therefore no upstream RNA primer or DNA), so DNA polymerase cannot function and genetic sequence might be lost through chromosomal fraying.

Examination of the pol genes that encode the DNA dependent DNA polymerase in various groups of viruses suggests a number of possible evolutionary relationships.

In 1986, Saiki started to use Thermophilus aquaticus (Taq) DNA polymerase to amplify segments of DNA.

Limited incorporation of the chain terminating nucleotide by the DNA polymerase results in a series of related DNA fragments that are terminated only at positions where that particular nucleotide is used.

Members of the family Bidnaviridae have evolved from insect parvoviruses by replacing the typical replication-initiation endonuclease with a protein-primed family B DNA polymerase acquired from large DNA transposons of the Polinton/Maverick family.

So the early procedures for DNA replication were very inefficient and time-consuming, and required large amounts of DNA polymerase and continuous handling throughout the process.

The second replication process occurs when host cellular DNA polymerase replicates the integrated viral DNA.

A complication at that point was that the DNA polymerase used was destroyed by the high heat used at the start of each replication cycle and had to be replaced.