Pol proteins are responsible for synthesis of viral DNA and integration into host DNA after infection.

In the final story arc of the season a human terrorist group, called Terra Prime, are bent on removing all non-humans from human planets and genetically engineer a child from DNA samples of Commander Tucker and Commander T ' Pol.

Pol β is required for short-patch base excision repair, a DNA repair pathway that is essential for repairing alkylated or oxidised bases as well as abasic sites.

Pol λ and Pol μ are involved in non-homologous end-joining, a mechanism for rejoining DNA double-strand breaks.

It was later learned that a terrorist group called Terra Prime had created the child by cloning a sample T ' Pol and Trip's DNA, which had been stolen from the Enterprise.

DNA Polymerase I ( or Pol I ) is an enzyme that participates in the process of DNA replication.

Pol I operates on RNA templates with considerably lower efficiency ( 0. 1 – 0. 4 %) than it does DNA templates, and this activity is probably of only limited biological significance.

These RNA oligonucleotides serve as primers for DNA synthesis by bacterial DNA polymerase Pol III.

The complex has high processivity ( i. e. the number of nucleotides added per binding event ) and, specifically referring to the replication of the E. coli genome, works in conjunction with four other DNA polymerases ( Pol I, Pol II, Pol IV, and Pol V ).

Being the primary holoenzyme involved in replication activity, the DNA Pol III holoenzyme also has proofreading capabilities that correct replication mistakes by means of exonuclease activity working 3 '-> 5 '.

DNA Pol III is a component of the replisome, which is located at the replication fork.

* 2 DNA Pol III enzymes, each comprising α, ε and θ subunits.

In E. coli, which replicates its entire genome from a single replication fork, the polymerase DNA Pol III is the enzyme primarily responsible for DNA replication and forms a replication complex with extremely high processivity.

The related DNA Pol I has exonuclease activity and serves to degrade the RNA primers used to initiate DNA synthesis.

Pol I then synthesizes the short DNA fragments that were formerly hybridized to the RNA fragment.

Several in vitro studies indicated that high concentrations of chromium ( III ) in the cell can lead to DNA damage.

The last mechanism attributed the genotoxicity to the binding to the DNA of the end product of the chromium ( III ) reduction.

* DNA ligase II: alternatively spliced form of DNA ligase III found in non-dividing cells.

* DNA ligase III: complexes with DNA repair protein XRCC1 to aid in sealing DNA during the process of nucleotide excision repair and recombinant fragments.

In higher eukaryotes and plants, the situation is more complex, for the 5S DNA sequence lies outside the NOR and is transcribed by RNA pol III in the nucleoplasm, after which it finds its way into the nucleolus to participate in the ribosome assembly.

** DNA polymerase III holoenzyme

Because DNA polymerase III cannot synthesize in the 3 '→ 5 ' direction, the lagging strand is synthesized in short segments known as Okazaki fragments.

Naturally occurring restriction endonucleases are categorized into four groups ( Types I, II III, and IV ) based on their composition and enzyme cofactor requirements, the nature of their target sequence, and the position of their DNA cleavage site relative to the target sequence.

Type III enzymes recognise short 5-6 bp long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5 ' protrusions.

The ICTV classifies RNA viruses as those that belong to Group III, Group IV or Group V of the Baltimore classification system of classifying viruses, and does not consider viruses with DNA intermediates in their life cycle as RNA viruses.

DNA Polymerase III alpha subunit from E. coli is the catalytic subunit and possesses no known nuclease activity.

For example, in cyanobacteria, DnaE, the catalytic subunit α of DNA polymerase III, is encoded by two separate genes, dnaE-n and dnaE-c.

Molecular phylogenetic analysis of DNA sequences has shown that Agapanthus is sister to a clade consisting of subfamilies Allioideae and Amaryllidoideae of the family Amaryllidaceae ( sensu APG III ).

This kind of staining is important especially to show proteins ( for example type III collagen ) and DNA.

It was not until the discovery of DNA polymerase III that the main replicative DNA polymerase was finally identified.

* DNA polymerase III

# REDIRECT DNA polymerase III holoenzyme

# REDIRECT DNA polymerase III holoenzyme

DNA polymerase III is then able to start DNA replication.

The limiting factor in blunt end ligation is not the activity of the ligase but rather the number of alignments between DNA fragment ends that occur.

# Normally RecA * binds LexA ( a transcription repressor ), activating LexA auto-protease activity, which destroys LexA repressor allowing production of DNA repair proteins.

However, the HIV-encoded reverse transcriptase has own ribonuclease activity that degrades the viral RNA during the synthesis of cDNA, as well as DNA-dependent DNA polymerase activity that copies the sense cDNA strand into an antisense DNA to form a double-stranded DNA intermediate.

The DNA double helix is unwound by the helicase activity of the enzyme.

Inside a bacterial host, the restriction enzymes selectively cut up foreign DNA in a process called restriction ; host DNA is methylated by a modification enzyme ( a methylase ) to protect it from the restriction enzyme ’ s activity.

Type I restriction enzymes possess three subunits called HsdR, HsdM, and HsdS ; HsdR is required for restriction ; HsdM is necessary for adding methyl groups to host DNA ( methyltransferase activity ) and HsdS is important for specificity of the recognition ( DNA-binding ) site in addition to both restriction ( DNA cleavage ) and modification ( DNA methyltransferase ) activity.

They recognize and cleave DNA at the same site, and they do not use ATP or AdoMet for their activity — they usually require only Mg < sup > 2 +</ sup > as a cofactor.

It also is a DNA-dependent DNA polymerase which synthesizes a second strand of DNA complementary to the reverse-transcribed single-stranded cDNA after degrading the original mRNA with its RNaseH activity.

In virus species with reverse transcriptase lacking DNA-dependent DNA polymerase activity, creation of double-stranded DNA can possibly be done by host-encoded DNA polymerase δ, mistaking the viral DNA-RNA for a primer and synthesizing a double-stranded DNA by similar mechanism as in primer removal, where the newly synthesized DNA displaces the original RNA template.