The fate of oocyte nuclear proteins during early development ofXenopus laevis

Dreyer, Christine; Scholz, Elke; Hausen, Peter; Gläser, Brigitte; Müller, Ursula; Siegel, Elisabeth

doi:10.1007/bf00848409

Cited by 74 publications

(24 citation statements)

References 9 publications

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“…Clearly, the nuclei in both the secretory epithelial cells of the stomach and gut, as well as the nuclei of the neural tube and spinal ganglia stain positive, whereas the nuclei of the pharyngobranchial cells show no detectable staining. The lack of staining with the antibody in the pharyngobranchial cells in the section shown in Figure 6E is not due to an artifact because these sections can be counterstained with a different antibody (see Dreyer et al 1982). The presence of protein xlgv7 in the stomach and gut is a transient phenomenon.…”

Section: Xlgv7 Is Expressed At the Neurula Stage And In Adult Brainmentioning

confidence: 92%

“…After oocyte maturation, the protein is dispersed into the cytoplasm and remains there during early development through the gastrula stage. At this time, protein xlgv7 reenters all nuclei of the embryo (Dreyer et al 1982). It is detected in all nuclei until late in development (stages 51 and onward) when it becomes localized in the nuclei of specific regions of the tadpole.…”

Section: Xlgv7 Is Expressed At the Neurula Stage And In Adult Brainmentioning

confidence: 97%

“…It corresponds to a protein of 591 amino acid residues with a calculated molecular weight of 75,200. We believe it to be the correct ORF because (1) it codes for a protein that is comparable to the molecular weight of protein xlgv7, which was determined by gel xlgv7: a neural-specific nuclear protein electrophoresis (Dreyer et al 1982); (2) no other ORF can encode a polypeptide of this size; and (3) RNA blots probed with single-stranded probes demonstrate that this reading frame is represented on the sense strand. There was no significant match to any protein or DNA sequences in the GenBank, EMBL, or NBRF data bases.…”

Section: Cloning and Characterization Of The Xlgv7 Cdnamentioning

confidence: 97%

“…The size-fractionated library had inserts ranging from 600 bp to >9 kb in length, with an average size of -2.0 kb, and contained -2 x 106 independent recombinants. The library was screened with the monoclonal antibody (mAb) 37-1A9 against protein 7 (Dreyer et al 1982). Three clones were isolated, two of which represented the same mRNA and contained inserts of -2.1 kb (xlgv7-1, xlgv7-2).…”

Section: Cloning and Characterization Of The Xlgv7 Cdnamentioning

confidence: 99%

“…It is possible that this protein may function in some way in the development of the CNS, as well as other structures during Xenopus development. We refer to this gene as xlgv7 because its product originates in the GV and corresponds to the protein referred to as 7 (Dreyer et al 1982).…”

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xlgv7: a maternal gene product localized in nuclei of the central nervous system in Xenopus laevis.

Miller¹,

Kloc²,

Reddy³

et al. 1989

Genes Dev.

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The Xenopus oocyte nucleus (GV) is a storehouse for a large number of proteins that are used during early development. We have cloned and characterized a cDNA coding for a maternal gene product that is localized in the GV and then becomes highly enriched in the nuclei of the central nervous system {CNS) of tadpoles and adult frogs. This cDNA {xlgv7) is 2.1 kb and hybridizes to a 2.4-kb RNA species on Northern blots. Southern blots of genomic DNA suggest that this gene is a member of a multigene family. The cDNA sequence reveals a long open reading frame (ORF) of 1773 nucleotides, with a putative nuclear targeting signal {Glu Arg Arg Lys Lys Lys Thr) at the extreme carboxyl terminus and an internal histidine {His)-rich region with a repeated conserved amino acid sequence between His pairs. The significance of this region is unclear, but the protein is a DNA-binding protein, and it is possible that this region is involved in this function. The xlgv7 protein also possesses a putative nucleotide-binding consensus sequence that is similar to the bacterial RecA and RecB and yeast RAD proteins. Protein xlgv7 exists as several isotypes that exhibit developmental and cellspecific changes during development. Northern blot analysis of the abundance of the xlgv7 mRNA shows an accumulation following neural induction at stages 15--16. There is a transient expression of the mRNA in the gut of tadpoles. In the adult, the mRNA is highly enriched in the brain and is absent or in very low abundance in other tissues. Immunohistochemical analysis of the protein shows that the protein is localized in the nuclei of the brain cells. We conclude that the xlgv7 gene product is a maternal protein that may serve several important functions, one of which may be in the development and maintanance of the CNS.

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Section: Xlgv7 Is Expressed At the Neurula Stage And In Adult Brainmentioning

confidence: 92%

Section: Xlgv7 Is Expressed At the Neurula Stage And In Adult Brainmentioning

confidence: 97%

Section: Cloning and Characterization Of The Xlgv7 Cdnamentioning

confidence: 97%

Section: Cloning and Characterization Of The Xlgv7 Cdnamentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

xlgv7: a maternal gene product localized in nuclei of the central nervous system in Xenopus laevis.

Miller¹,

Kloc²,

Reddy³

et al. 1989

Genes Dev.

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Transport across the nuclear envelope: Enigmas and explanations

Dingwall¹

1991

BioEssays

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The transport of molecules across the nuclear envelope plays a central role in the metabolism of the cell. Significant advances in three major areas highlight the limits of our current knowledge and point to the prospect of exciting future developments. Firstly, findings that ions and small proteins do not diffuse freely into the nucleus call into question the current views of nuclear envelope permeability. Secondly, indications that nuclear protein import can be regulated in conjunction with the cell cycle and development have been confirmed by the clear demonstration of regulated nuclear entry of specific transcription factors and morphogens. Thirdly, identification and characterisation of candidate receptor proteins indicates that the recognition of the nuclear targeting sequence occurs in the cytoplasm, suggesting that a different recognition event occurs at the nuclear pore.

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Nucleoplasmin cDNA sequence reveals polyglutamic acid tracts and a cluster of sequences homologous to putative nuclear localization signals.

Dingwall¹,

Dilworth²,

Black³

et al. 1987

The EMBO Journal

255

152

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Parks Road, Oxford OXI 3PS, UK Communicated by R. A.Laskey Nucleoplasmin is the most abundant protein in the Xenopus oocyte nucleus. It is involved in histone storage and chromatin assembly and it has been used extensively to study the transport of proteins into the cell nucleus. We have isolated X gtll phage containing nucleoplasmin cDNA and have determined the sequence of the entire protein coding region of 200 amino acids for one of the two genes. The translation product of the sp6 transcript of this cDNA has the same electrophoretic mobility as nucleoplasmin and is able to form pentamers. The protein sequence shows remarkable clusters of charged residues including a long polyglutamic acid tract which presumably constitutes the histone binding site. The short C-terminal domain which specifies nuclear entry contains four regions which are homologous to putative nuclear localization signals including two regions of homology to the nuclear migration signal of SV40 large T antigen.

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The fate of oocyte nuclear proteins during early development ofXenopus laevis

Cited by 74 publications

References 9 publications

xlgv7: a maternal gene product localized in nuclei of the central nervous system in Xenopus laevis.

xlgv7: a maternal gene product localized in nuclei of the central nervous system in Xenopus laevis.

Transport across the nuclear envelope: Enigmas and explanations

Nucleoplasmin cDNA sequence reveals polyglutamic acid tracts and a cluster of sequences homologous to putative nuclear localization signals.

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