The nucleic acid binding activity of nucleolar protein B23.1 resides in its carboxyl-terminal end.

@article{Wang1994TheNA,
  title={The nucleic acid binding activity of nucleolar protein B23.1 resides in its carboxyl-terminal end.},
  author={Dao Wen Wang and Arnd Baumann and Attila Szebeni and Mark O. J. Olson},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 49},
  pages={30994-8}
}
Protein B23 is a major nucleolar phosphoprotein proposed to be a ribosome assembly factor. Protein B23 exists as two isoforms, B23.1 and B23.2, differing only in their carboxyl-terminal sequences. The interaction of recombinantly produced B23 isoforms with double-stranded DNA was studied using gel retardation and nitrocellulose filter disk assays. Protein B23.1 bound saturably to radiolabeled plasmid DNA. By competition assays protein B23.1 was also capable of binding RNA and single-stranded… CONTINUE READING
35 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 35 extracted citations

Similar Papers

Loading similar papers…