The C-terminal domain of nucleolin accelerates nucleic acid annealing.
We report that the abundant nucleolar protein nucleolin accelerates nucleic acid annealing. Nucleolin accelerates annealing of complementary oligonucleotides and of oligonucleotides that contain a limited number of mismatches. The annealing activity of nucleolin can be localized to a C-terminal region consisting of two RNA binding domains (RBD3 and RBD4) and the RGG(9) domain (RBD3-RBD4-RGG(9)). This same region mediates self-association of nucleolin. The RGG(9) domain of nucleolin, believed to mediate interactions between nucleolin and several ribosomal proteins, is neither sufficient for self-association, as determined by small-angle X-ray scattering, nor can it independently accelerate annealing. Acceleration of nucleic acid annealing by nucleolin is likely to depend on self-association of nucleolin molecules bound to nucleic acid.
Hanakahi
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LA
Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut 06520-8024, USA. L.Hanakahi@icrf.icnet.uk
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D000818:Animals; D051379:Mice; D009687:Nuclear Proteins / Q000737:chemistry; D009696:Nucleic Acids / Q000737:chemistry / Q000378:metabolism; D010750:Phosphoproteins / Q000737:chemistry*; D016601:RNA-Binding Proteins / Q000737:chemistry*; D000097796:Nucleolin
D009687:Nuclear Proteins; D009696:Nucleic Acids; D010750:Phosphoproteins; D016601:RNA-Binding Proteins; D000097796:Nucleolin