Evidence map›Paper›PMID 3168999›Full record

ArticleThe EMBO journal1988

Identification of domains involved in nuclear uptake and histone binding of protein N1 of Xenopus laevis.

J A Kleinschmidt, A Seiter

Abstract read
In one paragraph

Article in The EMBO journal, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

40 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Engineered biological entities for drug delivery and gene therapy protein nanoparticles.Progress in molecular biology and translational science · 2011
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Peptide-guided gene delivery.The AAPS journal · 2007
    Review
  12. Article
  13. Mapping Hsp47 binding site(s) using CNBr peptides derived from type I and type II collagen.Protein science : a publication of the Protein Society · 2003
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

J A KleinschmidtInstitute of Cell and Tumor Biology, German Cancer Research Center, Heidelberg.
A Seiter

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The karyophilic protein N1 (590 amino acids) is an abundant soluble protein of the nuclei of Xenopus laevis oocytes where it forms defined complexes with histones H3 and H4. The amino acid sequence of this protein, as deduced from the cDNA, reveals a putative nuclear targeting signal as well as two acidic domains which are candidates for the interaction with histones. Using two different histone binding assays in vitro we have found that the deletion of the larger acidic domain reduces histone binding drastically to a residual value of approximately 15% of the complete molecule, whereas removal of the smaller acidic domain only slightly reduces histone complex formation in solution, but infers more effectively with binding to immobilized histones. In the primary structure of the protein both histone-binding domains are distant from the conspicuous nuclear accumulation signal sequence (residues 531-537) close to the carboxy terminus which is very similar to the SV40 large T-antigen nuclear targeting sequence. Using a series of N1 mutants altered by deletions or point mutations we show that this signal is required but not sufficient for nuclear accumulation of protein N1. The presence of an additional, more distantly related signal sequence in position 544-554 is also needed to achieve a level of nuclear uptake equivalent to that of the wild-type protein. Results obtained with point mutations support the concept of two nuclear targeting sequences and emphasize the importance of specific lysine and arginine residues in these signal sequences.

Indexed as

Amino Acid SequenceAnimalsBiological TransportCarrier ProteinsCell NucleusDNAFemaleHistonesMolecular Sequence DataNuclear ProteinsOocytesProtein BindingXenopus laevisCarrier ProteinsDNAHistonesN1-N2 protein, XenopusNuclear Proteins

Identifiers

PMID3168999
PMCPMC457143

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.