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A clone was isolated from a cDNA library from early embryos of Xenopus laevis that codes for a highly charged protein containing 339 amino acids. Two putative nuclear localization signals could be identified in its sequence, but no other known motifs or domains. Closely related ORFs are present in the genomes of man, C. elegans, yeast and Arabidopsis. A fusion protein with GFP expressed in HeLa cells or Xenopus oocytes was found to be localized in the nucleolus and coiled (Cajal) bodies. Moreover, immunoprecipitation experiments demonstrated that the new Xenopus protein interacts with 5S, 5.8S and 28S RNAs of large ribosomal subunits. The name Brix (biogenesis of ribosomes in Xenopus) is proposed for this protein and the corresponding gene. In Saccharomyces cerevisiae, the essential gene YOL077c, now named BRX1, codes for the Brix homolog, which is also localized in the nucleolus. Depletion of Brx1 p in a conditional yeast mutant leads to defects in rRNA processing, and a block in the assembly of large ribosomal subunits.

Original publication

DOI

10.1515/BC.2001.199

Type

Journal article

Journal

Biol Chem

Publication Date

12/2001

Volume

382

Pages

1637 - 1647

Keywords

Amino Acid Sequence, Animals, Base Sequence, Blotting, Northern, Cell Nucleolus, DNA, Ribosomal, Fluorescent Antibody Technique, HeLa Cells, Humans, Molecular Sequence Data, Precipitin Tests, RNA, Ribosomal, 28S, RNA, Ribosomal, 5.8S, RNA, Ribosomal, 5S, RNA-Binding Proteins, Ribosomal Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid, Xenopus laevis