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- W1508943571 abstract "One-dimensional diffusion is used by transcription factors and restriction endonucleases to locate specific sites on double-stranded DNA. The backbone of RNA, like that of DNA, could allow for the facilitated diffusion of proteins. Yet, the facilitated diffusion of a protein along RNA (or any single-stranded nucleic acid) has not been demonstrated so far. Single-stranded DNA is an excellent substrate analog for ribonuclease A (RNase A), and this analogy is the basis for the work described in the chapter. First, this chapter reports the use of DNA oligonucleotides and fluorescence polarization to probe the binding of adenine to the B1 subsite of RNase A. Then, it describes the use of DNA/RNA chimeric oligonucleotides to distinguish between three-dimensional and one-dimensional diffusion mechanisms for catalysis by RNase A. The results provide a biophysical rationale, as well as direct evidence for the diffusion of a protein along a single-stranded nucleic acid. Bovine pancreatic RNase A is a distributive endoribonuclease that catalyzes the cleavage of the P-O5′ bond of RNA on the 3′ side of pyrimidine residues. RNase A binds to polymeric substrates and can use one-dimensional diffusion along a poly(dA) tract to accelerate the location of a uridine substrate. Use of this mechanism depends on the concentration of NaCl, as expected if the enzyme is binding to the nucleic acid by nonspecific interactions with phosphoryl groups. Binding of the enzymic active site to adenosine residues is 20-fold weaker than uridine residues, which could enhance the ability of the enzyme to slide along the poly(dA) tract." @default.
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- W1508943571 date "1997-01-01" @default.
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- W1508943571 title "One-dimensional diffusion of a protein along a single-stranded nucleic acid" @default.
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- W1508943571 doi "https://doi.org/10.1016/s1080-8914(97)80056-7" @default.
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