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Details on Person The remaining flap, which is too short to support RPA bindin...

Class:Id	Summation:69153
_displayName	The remaining flap, which is too short to support RPA bindin...
_timestamp	2011-12-22 15:21:58
literatureReference	[LiteratureReference:69154] CalfRTH-1 nuclease can remove the initiator RNAs of Okazaki fragments by endonuclease activity. [LiteratureReference:69158] The FEN-1 family of structure-specific nucleases in eucaryotic DNA replication, recombination and repair. [LiteratureReference:69160] DNA structural elements required for FEN-1 binding. [LiteratureReference:69162] The characterization of a mammalian DNA structure-specific endonuclease. [LiteratureReference:69163] A comparison of eubacterial and archaeal structure-specific 5'-endonucleases. [LiteratureReference:68353] Cleavage specificity of Saccharomyces cerevisiae flap endonuclease 1 suggests a double-flap structure as the cellular substrate. [LiteratureReference:68358] Coordination between the polymerase and 5'-nuclease components of DNA polymerase I of Escherichia coli.
modified	[InstanceEdit:183139] Gillespie, ME, 2006-07-21 18:01:36 [InstanceEdit:2026123] Orlic-Milacic, M, 2011-12-22
text	The remaining flap, which is too short to support RPA binding, is then processed by FEN-1. There is evidence that binding of RPA to the displaced end of the RNA-containing Okazaki fragment prevents FEN-1 from accessing the substrate. FEN-1 is a structure-specific endonuclease that cleaves near the base of the flap at a position one nucleotide into the annealed region. Biochemical studies have shown that the preferred substrate for FEN-1 consists of a one-nucleotide 3'-tail on the upstream primer in addition to the 5'-flap of the downstream primer.
(summation)	[Reaction:69152] Removal of remaining Flap [Homo sapiens]
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