FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2085486557> ?p ?o ?g. }

• W2085486557 endingPage "1015" @default.
• W2085486557 startingPage "1008" @default.
• W2085486557 abstract "The EcoRV methyltransferase modifies DNA by the introduction of a methyl group at the 6-NH2 position of the first deoxyadenosine in GATATC sequences. The enzyme forms a stable and specific complex with GATATC sequences in the presence of a nonreactive analogue, such as sinefungin, of its natural cofactor S-adenosyl-L-methionine. Using circular permutation band mobility shift analysis (in which the distance between the GATATC sequence and the end of the DNA is varied) of protein-DNA-cofactor complexes we have shown the methylase induces a bend of just over 60° in the bound DNA. This was confirmed by phasing analysis, in which the spacing between the GATATC site and a poly(dA) tract is varied through a helical turn, which showed that the orientation of the induced curve was toward the major groove. There was no significant difference in the bend angle measured using unmethylated GATATC sequences and hemimethylated sequences which contain G6-MeATATC in one strand only. These are the natural substrates for the enzyme. The EcoRV endonuclease, a very well characterized protein, served as a positive control. DNA bending by this protein has been previously determined both by crystallographic and solution methods. The two proteins bend DNA toward the major groove but the bend angle produced by the methylase, slightly greater than 60°, is a little larger than that observed with the endonuclease, which is approximately 44°. The EcoRV methyltransferase modifies DNA by the introduction of a methyl group at the 6-NH2 position of the first deoxyadenosine in GATATC sequences. The enzyme forms a stable and specific complex with GATATC sequences in the presence of a nonreactive analogue, such as sinefungin, of its natural cofactor S-adenosyl-L-methionine. Using circular permutation band mobility shift analysis (in which the distance between the GATATC sequence and the end of the DNA is varied) of protein-DNA-cofactor complexes we have shown the methylase induces a bend of just over 60° in the bound DNA. This was confirmed by phasing analysis, in which the spacing between the GATATC site and a poly(dA) tract is varied through a helical turn, which showed that the orientation of the induced curve was toward the major groove. There was no significant difference in the bend angle measured using unmethylated GATATC sequences and hemimethylated sequences which contain G6-MeATATC in one strand only. These are the natural substrates for the enzyme. The EcoRV endonuclease, a very well characterized protein, served as a positive control. DNA bending by this protein has been previously determined both by crystallographic and solution methods. The two proteins bend DNA toward the major groove but the bend angle produced by the methylase, slightly greater than 60°, is a little larger than that observed with the endonuclease, which is approximately 44°." @default.
• W2085486557 created "2016-06-24" @default.
• W2085486557 creator A5013275706 @default.
• W2085486557 creator A5059665923 @default.
• W2085486557 date "1996-01-01" @default.
• W2085486557 modified "2023-10-13" @default.
• W2085486557 title "The EcoRV Modification Methylase Causes Considerable Bending of DNA upon Binding to Its Recognition Sequence GATATC" @default.
• W2085486557 cites W1473977991 @default.
• W2085486557 cites W1504799171 @default.
• W2085486557 cites W1555187143 @default.
• W2085486557 cites W1559480198 @default.
• W2085486557 cites W1564791373 @default.
• W2085486557 cites W1593479774 @default.
• W2085486557 cites W1595624904 @default.
• W2085486557 cites W1973763076 @default.
• W2085486557 cites W1975012397 @default.
• W2085486557 cites W1981929180 @default.
• W2085486557 cites W1983194324 @default.
• W2085486557 cites W1985459186 @default.
• W2085486557 cites W1986586522 @default.
• W2085486557 cites W1987587101 @default.
• W2085486557 cites W1994162276 @default.
• W2085486557 cites W1994762770 @default.
• W2085486557 cites W1997974036 @default.
• W2085486557 cites W2000215876 @default.
• W2085486557 cites W2005675760 @default.
• W2085486557 cites W2006408340 @default.
• W2085486557 cites W2011353224 @default.
• W2085486557 cites W2011897495 @default.
• W2085486557 cites W2012461974 @default.
• W2085486557 cites W2019114462 @default.
• W2085486557 cites W2024101862 @default.
• W2085486557 cites W2026598193 @default.
• W2085486557 cites W2029503268 @default.
• W2085486557 cites W2029602153 @default.
• W2085486557 cites W2032864324 @default.
• W2085486557 cites W2034258382 @default.
• W2085486557 cites W2035797443 @default.
• W2085486557 cites W2036001656 @default.
• W2085486557 cites W2036272159 @default.
• W2085486557 cites W2037928324 @default.
• W2085486557 cites W2038003996 @default.
• W2085486557 cites W2038874225 @default.
• W2085486557 cites W2042900296 @default.
• W2085486557 cites W2048562981 @default.
• W2085486557 cites W2050728905 @default.
• W2085486557 cites W2051064236 @default.
• W2085486557 cites W2053099555 @default.
• W2085486557 cites W2053561906 @default.
• W2085486557 cites W2059401090 @default.
• W2085486557 cites W2065367918 @default.
• W2085486557 cites W2071062575 @default.
• W2085486557 cites W2073038177 @default.
• W2085486557 cites W2077890483 @default.
• W2085486557 cites W2078085951 @default.
• W2085486557 cites W2081421427 @default.
• W2085486557 cites W2084015439 @default.
• W2085486557 cites W2086270305 @default.
• W2085486557 cites W2086275795 @default.
• W2085486557 cites W2087431455 @default.
• W2085486557 cites W2090949651 @default.
• W2085486557 cites W2091079122 @default.
• W2085486557 cites W2095294234 @default.
• W2085486557 cites W2098089372 @default.
• W2085486557 cites W2099195408 @default.
• W2085486557 cites W2145832687 @default.
• W2085486557 cites W2147562836 @default.
• W2085486557 cites W2197519829 @default.
• W2085486557 cites W3021884971 @default.
• W2085486557 cites W30415900 @default.
• W2085486557 cites W90350043 @default.
• W2085486557 doi "https://doi.org/10.1074/jbc.271.2.1008" @default.
• W2085486557 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8557624" @default.
• W2085486557 hasPublicationYear "1996" @default.
• W2085486557 type Work @default.
• W2085486557 sameAs 2085486557 @default.
• W2085486557 citedByCount "21" @default.
• W2085486557 countsByYear W20854865572012 @default.
• W2085486557 countsByYear W20854865572015 @default.
• W2085486557 countsByYear W20854865572018 @default.
• W2085486557 crossrefType "journal-article" @default.
• W2085486557 hasAuthorship W2085486557A5013275706 @default.
• W2085486557 hasAuthorship W2085486557A5059665923 @default.
• W2085486557 hasBestOaLocation W20854865571 @default.
• W2085486557 hasConcept C100594029 @default.
• W2085486557 hasConcept C128319531 @default.
• W2085486557 hasConcept C130123407 @default.
• W2085486557 hasConcept C185592680 @default.
• W2085486557 hasConcept C2776777567 @default.
• W2085486557 hasConcept C2780636463 @default.
• W2085486557 hasConcept C33288867 @default.
• W2085486557 hasConcept C552990157 @default.
• W2085486557 hasConcept C55493867 @default.
• W2085486557 hasConcept C71240020 @default.
• W2085486557 hasConcept C8010536 @default.
• W2085486557 hasConcept C86803240 @default.
• W2085486557 hasConcept C91965660 @default.
• W2085486557 hasConceptScore W2085486557C100594029 @default.

• next