Matches in SemOpenAlex for { <https://semopenalex.org/work/W2061781942> ?p ?o ?g. }
Showing items 1 to 87 of
87
with 100 items per page.
- W2061781942 endingPage "1233" @default.
- W2061781942 startingPage "1223" @default.
- W2061781942 abstract "A type II topoisomerase is essential for decatenating DNA replication products, and it accomplishes this task by passing one DNA duplex through a transient break in a second duplex. The B' domain of topoisomerase II contains three highly conserved motifs, EGDSA, PL(R/K)GK(I/L/M)LNVR, and IMTD(Q/A)DXD. We have investigated these motifs in topoisomerase II beta by mutagenesis, and report that they play a critical role in establishing the DNA cleavage-religation equilibrium. In addition, the mutations E477Q (EGDSA) and K505E (PLRGKILNVR) increase the optimal magnesium ion concentration for strand passage, without affecting the Mg(2+) dependence of ATP hydrolysis. It is likely that the binding affinity of the magnesium ion(s) specifically required for DNA cleavage has been reduced by these mutations. The crystal structure of yeast topo II indicates that residues E477 and K505 may help to position the three aspartate residues of the IMTD(Q/A)DXD motif for magnesium ion coordination, and we propose two possible locations for the magnesium ion binding site(s). These observations are consistent with a previous model in which the B' domain is positioned such that these acidic residues lie next to the active site tyrosine residue. A magnesium ion bound by these aspartate residues could therefore mediate the DNA cleavage-religation reaction." @default.
- W2061781942 created "2016-06-24" @default.
- W2061781942 creator A5016355890 @default.
- W2061781942 creator A5017919717 @default.
- W2061781942 creator A5022208465 @default.
- W2061781942 creator A5051825931 @default.
- W2061781942 creator A5066091943 @default.
- W2061781942 creator A5091850694 @default.
- W2061781942 date "2000-01-19" @default.
- W2061781942 modified "2023-09-26" @default.
- W2061781942 title "Mutagenesis of E477 or K505 in the B‘ Domain of Human Topoisomerase IIβ Increases the Requirement for Magnesium Ions during Strand Passage" @default.
- W2061781942 cites W1503908411 @default.
- W2061781942 cites W1519899019 @default.
- W2061781942 cites W1544840202 @default.
- W2061781942 cites W1594161662 @default.
- W2061781942 cites W1606546816 @default.
- W2061781942 cites W2057884054 @default.
- W2061781942 cites W2068598189 @default.
- W2061781942 cites W29362848 @default.
- W2061781942 doi "https://doi.org/10.1021/bi991328b" @default.
- W2061781942 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10684600" @default.
- W2061781942 hasPublicationYear "2000" @default.
- W2061781942 type Work @default.
- W2061781942 sameAs 2061781942 @default.
- W2061781942 citedByCount "35" @default.
- W2061781942 countsByYear W20617819422012 @default.
- W2061781942 countsByYear W20617819422013 @default.
- W2061781942 countsByYear W20617819422015 @default.
- W2061781942 countsByYear W20617819422016 @default.
- W2061781942 countsByYear W20617819422017 @default.
- W2061781942 countsByYear W20617819422018 @default.
- W2061781942 countsByYear W20617819422019 @default.
- W2061781942 crossrefType "journal-article" @default.
- W2061781942 hasAuthorship W2061781942A5016355890 @default.
- W2061781942 hasAuthorship W2061781942A5017919717 @default.
- W2061781942 hasAuthorship W2061781942A5022208465 @default.
- W2061781942 hasAuthorship W2061781942A5051825931 @default.
- W2061781942 hasAuthorship W2061781942A5066091943 @default.
- W2061781942 hasAuthorship W2061781942A5091850694 @default.
- W2061781942 hasConcept C12554922 @default.
- W2061781942 hasConcept C147897179 @default.
- W2061781942 hasConcept C151730666 @default.
- W2061781942 hasConcept C175156509 @default.
- W2061781942 hasConcept C178790620 @default.
- W2061781942 hasConcept C185592680 @default.
- W2061781942 hasConcept C43369102 @default.
- W2061781942 hasConcept C543218039 @default.
- W2061781942 hasConcept C552990157 @default.
- W2061781942 hasConcept C55493867 @default.
- W2061781942 hasConcept C71240020 @default.
- W2061781942 hasConcept C8010536 @default.
- W2061781942 hasConcept C86803240 @default.
- W2061781942 hasConceptScore W2061781942C12554922 @default.
- W2061781942 hasConceptScore W2061781942C147897179 @default.
- W2061781942 hasConceptScore W2061781942C151730666 @default.
- W2061781942 hasConceptScore W2061781942C175156509 @default.
- W2061781942 hasConceptScore W2061781942C178790620 @default.
- W2061781942 hasConceptScore W2061781942C185592680 @default.
- W2061781942 hasConceptScore W2061781942C43369102 @default.
- W2061781942 hasConceptScore W2061781942C543218039 @default.
- W2061781942 hasConceptScore W2061781942C552990157 @default.
- W2061781942 hasConceptScore W2061781942C55493867 @default.
- W2061781942 hasConceptScore W2061781942C71240020 @default.
- W2061781942 hasConceptScore W2061781942C8010536 @default.
- W2061781942 hasConceptScore W2061781942C86803240 @default.
- W2061781942 hasIssue "6" @default.
- W2061781942 hasLocation W20617819421 @default.
- W2061781942 hasLocation W20617819422 @default.
- W2061781942 hasOpenAccess W2061781942 @default.
- W2061781942 hasPrimaryLocation W20617819421 @default.
- W2061781942 hasRelatedWork W111117587 @default.
- W2061781942 hasRelatedWork W1994240050 @default.
- W2061781942 hasRelatedWork W2003454569 @default.
- W2061781942 hasRelatedWork W2026206582 @default.
- W2061781942 hasRelatedWork W2056339837 @default.
- W2061781942 hasRelatedWork W2075488730 @default.
- W2061781942 hasRelatedWork W2091661991 @default.
- W2061781942 hasRelatedWork W2152990948 @default.
- W2061781942 hasRelatedWork W2414295763 @default.
- W2061781942 hasRelatedWork W2129036898 @default.
- W2061781942 hasVolume "39" @default.
- W2061781942 isParatext "false" @default.
- W2061781942 isRetracted "false" @default.
- W2061781942 magId "2061781942" @default.
- W2061781942 workType "article" @default.