BASE FLIPPING

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On base flipping

Although change and adaptation are key to life, nature is reluctant to abandon old inventions. Even today when the hypothetical RNA world of our ancestors has been supplanted by the richer possibilities offered by proteins, we still find key processes catalyzed by RNA. Perhaps the oldest discovery was the unique power of base pairing to enable replication. This must have been key to the develop...

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DNA base flipping by a base pair-mimic nucleoside

On the basis of non-covalent bond interactions in nucleic acids, we synthesized the deoxyadenosine derivatives tethering a phenyl group (X) and a naphthyl group (Z) by an amide linker, which mimic a Watson-Crick base pair. Circular dichroism spectra indicated that the duplexes containing X and Z formed a similar conformation regardless of the opposite nucleotide species (A, G, C, T and an abasi...

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Simultaneous DNA Binding, Bending, and Base Flipping

We measured the kinetics of DNA bending by M.EcoRI using DNA labeled at both 5 -ends and observed changes in fluorescence resonance energy transfer. Although known to bend its cognate DNA site, energy transfer is decreased upon enzyme binding. This unanticipated effect is shown to be robust because we observe the identical decrease with different dye pairs, when the dye pairs are placed on the ...

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Base flipping in nucleotide excision repair.

UvrB, the ultimate damage-binding protein in bacterial nucleotide excision repair is capable of binding a vast array of structurally unrelated lesions. A beta-hairpin structure in the protein plays an important role in damage-specific binding. In this paper we have monitored DNA conformational alterations in the UvrB-DNA complex, using the fluorescent adenine analogue 2-aminopurine. We show tha...

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The coupling of tight DNA binding and base flipping: identification of a conserved structural motif in base flipping enzymes.

Val(121) is positioned immediately above the extrahelical cytosine in HhaI DNA C(5)-cytosine methyltransferase, and replacement with alanine dramatically interferes with base flipping and catalysis. DNA binding and k(cat) are decreased 10(5)-fold for the Val(121) --> Ala mutant that has a normal circular dichroism spectrum and AdoMet affinity. The magnitude of this loss of function is comparabl...

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ژورنال

عنوان ژورنال: Annual Review of Biochemistry

سال: 1998

ISSN: 0066-4154,1545-4509

DOI: 10.1146/annurev.biochem.67.1.181