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DNA polymerase's ability to slide along the DNA template allows increased processivity. There is a dramatic increase in processivity at the replication fork. This increase is facilitated by the DNA polymerase's association with proteins known as the sliding DNA clamp. The clamps are multiple protein subunits associated in the shape of a ring.
77782 Ensembl ENSG00000051341 ENSMUSG00000034206 UniProt O75417 Q8CGS6 RefSeq (mRNA) NM_199420 NM_006596 NM_001159369 NM_029977 RefSeq (protein) NP_955452 NP_001152841 NP_084253 Location (UCSC) Chr 3: 121.43 – 121.55 Mb Chr 16: 36.83 – 36.92 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse DNA polymerase theta is an enzyme that in humans is encoded by the POLQ gene. This ...
Afterwards, the 3’ ssDNA invades the template DNA, and displaces a DNA strand to form a D-loop. DNA polymerase and other accessory factors follows by replacing the missing DNA via DNA synthesis. Ligase then attaches the DNA strand break, [10] resulting in the formation of 2 Holliday junctions. The recombined DNA strands then undergoes ...
Microhomology-mediated end joining (MMEJ), also known as alternative nonhomologous end-joining (Alt-NHEJ) is one of the pathways for repairing double-strand breaks in DNA. As reviewed by McVey and Lee, [1] the foremost distinguishing property of MMEJ is the use of microhomologous sequences during the alignment of broken ends before joining, thereby resulting in deletions flanking the original ...
Melanoma cells are commonly defective in postreplication repair of DNA damages that are in the form of cyclobutane pyrimidine dimers, a type of damage caused by ultraviolet radiation. [ 11 ] [ 12 ] A particular repair process that appears to be defective in melanoma cells is homologous recombinational repair. [ 12 ]
During the replication of DNA, for example, the DNA polymerase I leaves behind a hole between the phosphates in the newly formed backbone. DNA ligase is able to form a phosphodiester bond between the nucleotides on each side of the gap. [2] Phosphodiesters are negatively charged at pH 7. [5]
Non-homologous end joining (NHEJ) is a pathway that repairs double-strand breaks in DNA. It is called "non-homologous" because the break ends are directly ligated without the need for a homologous template, in contrast to homology directed repair (HDR), which requires a homologous sequence to guide repair.
The crystal structure of pol λ shows that, unlike the DNA polymerases that catalyze DNA replication, pol λ makes extensive contacts with the 5' phosphate of the downstream DNA strand. This allows the polymerase to stabilize the two ends of a double-strand break and explains how pol λ is uniquely suited for a role in non-homologous end joining.