Nucleolin from Xenopus laevis: cDNA cloning and expression during development.

Caizergues‐Ferrer, Michèle; Mariottini, Paolo; Curie, Catherine; Lapeyre, Bruno; Gas, Nicole; Amalríc, François; Amaldi, Francesco

doi:10.1101/gad.3.3.324

Cited by 102 publications

(69 citation statements)

References 51 publications

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“…The fourth domain has the greatest conservation of sequence between species as recently reported in a comparison of the rodent and Xenopus sequences [36]. A glycine-rich carboxy-terminal domain (position 648-703) is also conserved and may be involved in proteinprotein and/or protein-nucleic acid interactions [37].…”

Section: Nucleolin Structure and Functionmentioning

confidence: 79%

Cloning and sequencing of the human nucleolin cDNA

et al. 1989

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A cDNA containing the entire coding region for human nucleolin has been isolated from a 1 gtl0 human retinal library using a bovine cDNA probe. The cDNA hybridized to a transcript of 3000 bases from fast-dividing cells, as well as terminally differentiated tissues of several species. Translation of the nucleotide sequence revealed a long open reading frame which predicts a 707 amino acid protein with several distinct domains. These include repeating elements, four conserved RNA-binding regions, a glycine-rich carboxy-terminal domain and sites for phosphorylation, glycosylation and dibasic cleavage. Human and bovine nucleolin exhibited more additions and/or substitutions of aspartate, glutamate and serine residues in the chromatin-binding domains by comparison with the hamster and mouse nucleolins. These differences may be related to species-specific functions in transcription.

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Section: Nucleolin Structure and Functionmentioning

confidence: 79%

Cloning and sequencing of the human nucleolin cDNA

et al. 1989

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“…2B). An N-terminal domain of -90 amino acid residues containing the two conserved consensus sequences called RNP1 and RNP2 (6) (1,37,68,87), nucleolins (15,19,53,77), small nuclear and heterogeneous nuclear ribonucleoparticles [snRNPs and hnRNPs, respectively [31,38,51,75,78]), and other single-stranded nucleic acid-binding proteins (see reference 6 for a review). This domain seems to be implicated in binding to the RNA molecule, albeit yeast cells containing a modified PABP, with a single domain lacking the octapeptide consensus RNP1, were able to grow (70).…”

Section: Resultsmentioning

confidence: 99%

“…SCPABP, HUPABP, and XENPABP are the poly(A)-binding proteins S. cerevisiae (1, 68), human (37), and Xenopus laevis (87), PABPs, respectively. HAMSNUCL, HUNUCL, XENNUCL, and CHICKNUCL are the hamster (53), human (77), Xenopus (19), and chicken (15) nucleolins, respectively. FLYHELDESTAB represents the Drosophila helix-destabilizing protein (40), homologous to the rat helix-destabilizing protein (25) (RATHELDESTAB).…”

Section: Amktkepveek-----irvool Dpnaqgdafk-----t Lrvarv Q-naqgdafk---mentioning

confidence: 99%

Mutations in the yeast RNA14 and RNA15 genes result in an abnormal mRNA decay rate; sequence analysis reveals an RNA-binding domain in the RNA15 protein.

Minvielle‐Sebastia¹,

Winsor²,

Bonneaud³

et al. 1991

Mol. Cell. Biol.

126

110

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In Saccharomyces cerevisiae, temperature-sensitive mutations in the genes RNA14 and RNA15 correlate with a reduction of mRNA stability and poly(A) tail length. Although mRNA transcription is not abolished in these mutants, the transcripts are rapidly deadenylated as in a strain carrying an RNA polymerase B(II) temperature-sensitive mutation. This suggests that the primary defect could be in the control of the poly(A) status of the mRNAs and that the fast decay rate may be due to the loss of this control. By complementation of their temperature-sensitive phenotype, we have cloned the wild-type genes. They are essential for cell viability and are unique in the haploid genome. The RNA14 gene, located on chromosome II, is transcribed as three mRNAs, one major and two minor, which are 2.2, 1.5, and 1.1 kb in length. The RNA15 gene gives rise to a single 1.2-kb transcript and maps to chromosome XVI. Sequence analysis indicates that RNA14 encodes a 636-amino-acid protein with a calculated molecular weight of 75,295. No homology was found between RNA14 and RNA15 or between RNA14 and other proteins contained in data banks. The RNA15 DNA sequence predicts a protein of 296 amino acids with a molecular weight of 32,770. Sequence comparison reveals an N-terminal putative RNA-binding domain in the RNA15-encoded protein, followed by a glutamine and asparagine stretch similar to the opa sequences. Both RNA14 and RNA15 wild-type genes, when cloned on a multicopy plasmid, are able to suppress the temperature-sensitive phenotype of strains bearing either the rnal4 or the rnal5 mutation, suggesting that the encoded proteins could interact with each other.In yeast cells, all known mRNAs terminate in a poly(A) tail that is probably added to the 3' end of the pre-mature RNA in the nucleus in a posttranscriptional manner (18), as was previously shown to be the case in higher eucaryotes (57). One of the major roles for the poly(A) tail was suggested by its involvement in protein biosynthesis (47,63), and in yeast cells the poly(A)-binding protein (PABP [1,68]) was shown to be required for translation initiation (69). More recently, in vitro data have supported the idea that the poly(A) tail enhances translation through the interaction of an initiation factor or the ribosomal subunit with the PABP (59).Besides the implication of the poly(A) tail in translation (reviewed in reference 46), its role in mRNA half-life has been evoked as many times (30,44,82,83,86), sometimes in association with the PABP (11, 12, 17), as refuted (41,49,69,72). Nevertheless, it appears that the poly(A) tail is not solely responsible for determination of the stability of mRNA in vivo, but that it acts in association with other factors.To obtain mutants of Saccharomyces cerevisiae impaired in poly(A) mRNA metabolism, two mutants simultaneously cordycepin (3'-deoxyadenosine) sensitive and temperature sensitive were isolated by using a selective approach (13). The mutations, located at two independent loci, were renamed rnal4 and rnal5 for reasons of homonymy (see...

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“…2). Furthermore, the inventory of nucleolar proteins is still growing and the function of even abundant nucleolar proteins such as N038jB23, a member of the nucleoplasmin family (29), nucleolinjC23 (32,33), and skeletal structural elements (34,35) is unknown.…”

Section: An Outline Of Nucleolus Organizationmentioning

confidence: 99%

Functional and dynamic aspects of the mammalian nucleolus

1990

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Nucleoli are the sites of ribosome biogenesis. Transcription of the ribosomal RNA genes as well as processing and initial packaging of their transcripts with ribosomal and non‐ribosomal proteins all occur within the nucleolus in an ordered manner and under defined topological conditions. Components of the nucleolus have been localized by immunocytochemistry and their functional aspects investigated by microinjection of antibodies directed against the enzyme responsible for rDNA transcription, RNA polymerase I. The role of nascent transcripts in postmitotic formation of nucleoli will be discussed.

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Nucleolin from Xenopus laevis: cDNA cloning and expression during development.

Cited by 102 publications

References 51 publications

Cloning and sequencing of the human nucleolin cDNA

Cloning and sequencing of the human nucleolin cDNA

Mutations in the yeast RNA14 and RNA15 genes result in an abnormal mRNA decay rate; sequence analysis reveals an RNA-binding domain in the RNA15 protein.

Functional and dynamic aspects of the mammalian nucleolus

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