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• W1983453394 endingPage "245" @default.
• W1983453394 startingPage "233" @default.
• W1983453394 abstract "During the first steps of site-specific recombination, Cre protein cleaves and religates a specific homologous pair of LoxP strands to form a Holliday junction (HJ) intermediate. The HJ is resolved into recombination products through exchange of the second homologous strand pair. CreH289A, containing a His to Ala substitution in the conserved R-H-R catalytic motif, has a 150-fold reduced recombination rate and accumulates HJs. However, to produce these HJs, CreH289A exchanges the opposite set of strands compared to wild-type Cre (CreWT). To investigate how CreH289A and CreWT impose strand exchange order, we characterized their reactivities and strand cleavage preferences toward LoxP duplex and HJ substrates containing 8bp spacer substitutions. Remarkably, CreH289A had different and often opposite strand exchange preferences compared to CreWT with nearly all substrates. CreH289N was much less perturbed, implying that overall recombination rate and strand exchange depend more on His289 hydrogen bonding capability than on its acid/base properties. LoxP substitutions immediately 5' (S1 nucleotide) or 3' (S1' nucleotide) of the scissile phosphate had large effects on substrate utilization and strand exchange order. S1' substitutions, designed to alter base-unstacking events concomitant with Cre-induced LoxP bending, caused HJ accumulation and dramatically inverted the cleavage preferences. That pre-formed HJs were resolved via either strand in vitro suggests that inhibition of the conformational switch isomerization required to trigger the second strand exchange accounts for the observed HJ accumulation. Rather than reflecting CreWT behavior, CreH289A accumulates HJs of opposite polarity through a combination of its unique cleavage specificity and an HJ isomerization defect. The overall implication is that cleavage specificity is mediated by sequence-dependent DNA deformations that influence the scissile phosphate positioning and reactivity. A role of His289 may be to selectively stabilize the activated phosphate conformation in order to promote cleavage." @default.
• W1983453394 created "2016-06-24" @default.
• W1983453394 creator A5015571057 @default.
• W1983453394 creator A5042484500 @default.
• W1983453394 creator A5048952715 @default.
• W1983453394 date "2005-11-01" @default.
• W1983453394 modified "2023-10-14" @default.
• W1983453394 title "Reversed DNA Strand Cleavage Specificity in Initiation of Cre–LoxP Recombination Induced by the His289Ala Active-site Substitution" @default.
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• W1983453394 doi "https://doi.org/10.1016/j.jmb.2005.08.077" @default.
• W1983453394 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2964137" @default.
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• W1983453394 hasPublicationYear "2005" @default.
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