A single-stranded nucleic acid-binding protein from Artemia salina. II. Interaction with nucleic acids.
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DOI: 10.1016/S0021-9258(18)43764-7
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摘要: Abstract A helix-destabilizing protein, HD40 (Mr 40,000), isolated from the cytoplasm of Artemia salina (Marvil, D.K., Nowak, L., and Szer, W. (1980) J. Biol. Chem. 255, 6466-6472) stoichiometrically disrupts secondary structures synthetic single-stranded helical polynucleotides (e.g. poly(rA), poly(dA), poly(rC), poly(dC), poly(rU)) as well those natural MS2 RNA phi X174 viral DNA). The conformations double-stranded DNA double- or triple-stranded are not affected by protein. Formation duplexes, e.g. poly(rA . rU), is prevented at 25 to 50 mM but 100 140 NaCl. unwinding residual structure highly cooperative has a stoichiometry one per 12 15 nucleotides. addition in excess 1 molecule nucleotides results formation distinct bead-like along nucleic acid strand. beads about 20 nm diameter with center distance 40 nm. appearance accompanied any spectral changes (CD UV) beyond obtained
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