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


ABSTRACT: We report the discovery and molecular characterization of a small and very acidic nucleolar protein of an SDS/PAGE mobility corresponding to Mr 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.

SUBMITTER: Zirwes RF 

PROVIDER: S-EPMC23475 | biostudies-literature | 1997 Oct

REPOSITORIES: biostudies-literature

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

Zirwes R F RF   Schmidt-Zachmann M S MS   Franke W W WW  

Proceedings of the National Academy of Sciences of the United States of America 19971001 21


We report the discovery and molecular characterization of a small and very acidic nucleolar protein of an SDS/PAGE mobility corresponding to Mr 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  ...[more]

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