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DNA helicases are frequently attracted to regions of DNA damage and are essential for cellular DNA replication, recombination, repair, and transcription. Chemical manipulation of their molecular processes can change the rate at which cancer cells divide, as well as, the efficiency of transactions and cellular homeostasis.
The replication fork is a structure that forms within the long helical DNA during DNA replication. It is produced by enzymes called helicases that break the hydrogen bonds that hold the DNA strands together in a helix.
The process of semiconservative replication for the site of DNA replication is a fork-like DNA structure, the replication fork, where the DNA helix is open, or unwound, exposing unpaired DNA nucleotides for recognition and base pairing for the incorporation of free nucleotides into double-stranded DNA. [3]
The double-stranded structure of DNA provides a simple mechanism for DNA replication. Here, the two strands are separated and then each strand's complementary DNA sequence is recreated by an enzyme called DNA polymerase. This enzyme makes the complementary strand by finding the correct base through complementary base pairing and bonding it onto ...
DNA is a duplex formed by two anti-parallel strands. Following Meselson-Stahl, the process of DNA replication is semi-conservative, whereby during replication the original DNA duplex is separated into two daughter strands (referred to as the leading and lagging strand templates). Each daughter strand becomes part of a new DNA duplex.
22427 Ensembl ENSG00000165392 ENSMUSG00000031583 UniProt Q14191 O09053 RefSeq (mRNA) NM_000553 NM_001122822 NM_011721 RefSeq (protein) NP_000544 NP_001116294 NP_035851 Location (UCSC) Chr 8: 31.03 – 31.18 Mb Chr 8: 33.72 – 33.88 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Werner syndrome ATP-dependent helicase, also known as DNA helicase, RecQ-like type 3, is an enzyme that ...
DnaB helicase is an enzyme in bacteria which opens the replication fork during DNA replication.Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerisation of the N-terminal domain has been observed and may occur during the enzymatic cycle. [1]
Stalled replication forks often lead to DNA breakage, further implicating the importance of unimpaired replication forks on genome integrity. [6] RRM3 helps cells progress through stalled replication forks, although this is a mechanism that is still poorly understood. [6] Rrm3p is one of many helicase proteins in Saccharomyces cerevisiae. Rrm3p ...