Dna2 of Saccharomyces cerevisiae possesses a single-stranded DNA-specific endonuclease activity that is able to act on double-stranded DNA in the presence of ATP.
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Isolation of human Dna2 endonuclease and characterization of its enzymatic propertiesBiochemical analysis of human Dna2Biochemical analyses indicate that binding and cleavage specificities define the ordered processing of human Okazaki fragments by Dna2 and FEN1DNA resection in eukaryotes: deciding how to fix the breakComponents of the secondary pathway stimulate the primary pathway of eukaryotic Okazaki fragment processingAn alternative pathway for Okazaki fragment processing: resolution of fold-back flaps by Pif1 helicaseOkazaki fragment maturation: nucleases take centre stageDNA end resection: many nucleases make light workEnzymatic properties of the Caenorhabditis elegans Dna2 endonuclease/helicase and a species-specific interaction between RPA and Dna2In vivo and in vitro studies of Mgs1 suggest a link between genome instability and Okazaki fragment processing.A network of multi-tasking proteins at the DNA replication fork preserves genome stabilityG-quadruplexes and helicasesDynamic localization of an Okazaki fragment processing protein suggests a novel role in telomere replicationSaccharomyces cerevisiae RNase H(35) functions in RNA primer removal during lagging-strand DNA synthesis, most efficiently in cooperation with Rad27 nucleaseDna2 mutants reveal interactions with Dna polymerase alpha and Ctf4, a Pol alpha accessory factor, and show that full Dna2 helicase activity is not essential for growthThe MPH1 gene of Saccharomyces cerevisiae functions in Okazaki fragment processing.POB3 is required for both transcription and replication in the yeast Saccharomyces cerevisiaeMutations in DNA replication genes reduce yeast life span.Involvement of Vts1, a structure-specific RNA-binding protein, in Okazaki fragment processing in yeast.Nuclease activity of Saccharomyces cerevisiae Dna2 inhibits its potent DNA helicase activity.Accumulation of single-stranded DNA and destabilization of telomeric repeats in yeast mutant strains carrying a deletion of RAD27.Single strand annealing and ATP-independent strand exchange activities of yeast and human DNA2: possible role in Okazaki fragment maturation.Interactions among DNA ligase I, the flap endonuclease and proliferating cell nuclear antigen in the expansion and contraction of CAG repeat tracts in yeastDna2p helicase/nuclease is a tracking protein, like FEN1, for flap cleavage during Okazaki fragment maturation.Sgs1 helicase and two nucleases Dna2 and Exo1 resect DNA double-strand break endsSURVEY AND SUMMARY: holliday junction resolvases and related nucleases: identification of new families, phyletic distribution and evolutionary trajectories.RPA governs endonuclease switching during processing of Okazaki fragments in eukaryotes.Bimodal interaction between replication-protein A and Dna2 is critical for Dna2 function both in vivo and in vitro.Dynamic removal of replication protein A by Dna2 facilitates primer cleavage during Okazaki fragment processing in Saccharomyces cerevisiaeThe protein components and mechanism of eukaryotic Okazaki fragment maturation.On the roles of Saccharomyces cerevisiae Dna2p and Flap endonuclease 1 in Okazaki fragment processing.Pif1 helicase directs eukaryotic Okazaki fragments toward the two-nuclease cleavage pathway for primer removal.Interplay of Mre11 nuclease with Dna2 plus Sgs1 in Rad51-dependent recombinational repair.Significance of the dissociation of Dna2 by flap endonuclease 1 to Okazaki fragment processing in Saccharomyces cerevisiae.Pif1 helicase lengthens some Okazaki fragment flaps necessitating Dna2 nuclease/helicase action in the two-nuclease processing pathway.The endonuclease activity of the yeast Dna2 enzyme is essential in vivo.Dna2 is a structure-specific nuclease, with affinity for 5'-flap intermediates.Rad52/Rad59-dependent recombination as a means to rectify faulty Okazaki fragment processing.Characterization of EndoTT, a novel single-stranded DNA-specific endonuclease from Thermoanaerobacter tengcongensisEnd resection at double-strand breaks: mechanism and regulation.
P2860
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P2860
Dna2 of Saccharomyces cerevisiae possesses a single-stranded DNA-specific endonuclease activity that is able to act on double-stranded DNA in the presence of ATP.
description
1998 nî lūn-bûn
@nan
1998 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Dna2 of Saccharomyces cerevisi ...... ed DNA in the presence of ATP.
@ast
Dna2 of Saccharomyces cerevisi ...... ed DNA in the presence of ATP.
@en
Dna2 of Saccharomyces cerevisi ...... ed DNA in the presence of ATP.
@nl
type
label
Dna2 of Saccharomyces cerevisi ...... ed DNA in the presence of ATP.
@ast
Dna2 of Saccharomyces cerevisi ...... ed DNA in the presence of ATP.
@en
Dna2 of Saccharomyces cerevisi ...... ed DNA in the presence of ATP.
@nl
prefLabel
Dna2 of Saccharomyces cerevisi ...... ed DNA in the presence of ATP.
@ast
Dna2 of Saccharomyces cerevisi ...... ed DNA in the presence of ATP.
@en
Dna2 of Saccharomyces cerevisi ...... ed DNA in the presence of ATP.
@nl
P2093
P2860
P3181
P356
P1476
Dna2 of Saccharomyces cerevisi ...... ed DNA in the presence of ATP.
@en
P2093
P2860
P304
P3181
P356
10.1074/JBC.273.41.26880
P407
P577
1998-10-09T00:00:00Z