title: The C-terminal domain of nucleolin accelerates nucleic acid annealing.
abstract: 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.
authors: 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
authors: L A
authors: LA
authors: Hanakahi
authors: Z
authors: Z
authors: Bu
authors: N
authors: N
authors: Maizels
mesh_terms: 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
chemical_list: D009687:Nuclear Proteins; D009696:Nucleic Acids; D010750:Phosphoproteins; D016601:RNA-Binding Proteins; D000097796:Nucleolin