The C-terminal domain of nucleolin accelerates nucleic acid annealing |
| |
Authors: | Hanakahi L A Bu Z Maizels N |
| |
Affiliation: | 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 |
| |
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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|