Molecular characterization of a novel, widespread nuclear protein that colocalizes with spliceosome components.

@article{SchmidtZachmann1998MolecularCO,
  title={Molecular characterization of a novel, widespread nuclear protein that colocalizes with spliceosome components.},
  author={Marion S. Schmidt-Zachmann and Sebastien Knecht and Angela Kr{\"a}mer},
  journal={Molecular biology of the cell},
  year={1998},
  volume={9 1},
  pages={143-60}
}
We report the identification and molecular characterization of a novel type of constitutive nuclear protein that is present in diverse vertebrate species, from Xenopus laevis to human. The cDNA-deduced amino acid sequence of the Xenopus protein defines a polypeptide of a calculated mass of 146.2 kDa and a isoelectric point of 6.8, with a conspicuous domain enriched in the dipeptide TP (threonine-proline) near its amino terminus. Immunolocalization studies in cultured cells and tissues sections… CONTINUE READING

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