Identification of a small, very acidic constitutive nucleolar protein (NO29) as a member of the nucleoplasmin family

Rudolf F. Zirwes, Marion S. Schmidt-Zachmann, Werner W. Franke

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Abstract

We report the discovery and molecular characterization of a small and very acidic nucleolar protein of an SDS/PAGE mobility corresponding to M(r) 29,000 (NO29). The cDNA-deduced sequence of the Xenopus laevis protein defines a polypeptide of a calculated molecular mass of 20,121 and a pI of 3.75, with an extended acidic region near its C terminus, and is related to the major nucleolar protein, NO38, and the histone-binding protein, nucleoplasmin. This member of the nucleoplasmin family of proteins was immunolocalized to nucleoli in Xenopus oocytes and diverse somatic cells. Protein NO29 is associated with nuclear particles from Xenopus oocytes, partly complexed with protein NO38, and occurs in preribosomes but not in mature ribosomes. The location and the enormously high content of negatively charged amino acids lead to the hypothesis that NO29 might be involved in the nuclear and nucleolar accumulation of ribosomal proteins and the coordinated assembly of pre-ribosomal particles.

Original languageEnglish (US)
Pages (from-to)11387-11392
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number21
DOIs
StatePublished - Oct 14 1997

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Nucleoplasmins
Nuclear Proteins
Xenopus
Oocytes
Xenopus Proteins
Proteins
Ribosomal Proteins
Ribosomes
Histones
Polyacrylamide Gel Electrophoresis
Carrier Proteins
Complementary DNA
Amino Acids
Peptides

ASJC Scopus subject areas

  • General

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Identification of a small, very acidic constitutive nucleolar protein (NO29) as a member of the nucleoplasmin family. / Zirwes, Rudolf F.; Schmidt-Zachmann, Marion S.; Franke, Werner W.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 94, No. 21, 14.10.1997, p. 11387-11392.

Research output: Contribution to journalArticle

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