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This helicase was described as a "DNA unwinding enzyme" that is "found to denature DNA duplexes in an ATP-dependent reaction, without detectably degrading". [13] The first eukaryotic DNA helicase discovered was in 1978 in the lily plant. [14]
Werner syndrome ATP-dependent helicase, also known as DNA helicase, RecQ-like type 3, is an enzyme that in humans is encoded by the WRN gene. WRN is a member of the RecQ Helicase family. [ 5 ] Helicase enzymes generally unwind and separate double-stranded DNA .
ATP-dependent DNA helicase Q1 is an enzyme that in humans is encoded by the RECQL gene. [5] [6] [7] The protein encoded by this gene is a member of the RecQ DNA helicase family. DNA helicases are enzymes involved in various types of DNA repair, including mismatch repair, nucleotide excision repair and direct repair.
RecQ helicase is a family of helicase enzymes initially found in Escherichia coli [1] that has been shown to be important in genome maintenance. [2] [3] [4] They function through catalyzing the reaction ATP + H 2 O → ADP + P and thus driving the unwinding of paired DNA and translocating in the 3' to 5' direction.
170472 Ensembl ENSG00000108469 ENSMUSG00000020752 UniProt O94762 Q8VID5 RefSeq (mRNA) NM_001003715 NM_001003716 NM_004259 NM_130454 RefSeq (protein) NP_001003715 NP_001003716 NP_004250 NP_569721 Location (UCSC) Chr 17: 75.63 – 75.67 Mb Chr 11: 115.78 – 115.82 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse ATP-dependent DNA helicase Q5 is an enzyme that in humans is encoded by ...
79456 Ensembl ENSG00000160957 ENSMUSG00000033762 UniProt O94761 Q75NR7 RefSeq (mRNA) NM_004260 NM_058214 RefSeq (protein) NP_004251 NP_478121 Location (UCSC) Chr 8: 144.51 – 144.52 Mb Chr 15: 76.59 – 76.59 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse ATP-dependent DNA helicase Q4 is an enzyme that in humans is encoded by the RECQL4 gene. Mutations in RECQL4 are associated with ...
When the progress of the replication fork is impeded the proteins single-stranded binding protein SSB and RecG helicase along with the RuvABC complex are required for rescue. [2] The resolution of Holliday junctions that accumulate following replication on damaged DNA templates in E. coli requires the RuvABC complex. [3]
This model is based on reactions of DNA and RecBCD with ATP in excess over Mg2+ ions. Step 1: RecBCD binds to a double-stranded DNA end. Step 2: RecBCD unwinds DNA. RecD is a fast helicase on the 5’-ended strand, and RecB is a slower helicase on the 3'-ended strand (that with an arrowhead) [ref 46 in current Wiki version].
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