Evidence map›Paper›PMID 3549279›Full record

ArticleThe EMBO journal1986

Molecular characterization of a karyophilic, histone-binding protein: cDNA cloning, amino acid sequence and expression of nuclear protein N1/N2 of Xenopus laevis.

J A Kleinschmidt, C Dingwall, G Maier, W W Franke

Abstract read
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Article in The EMBO journal, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

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63citing papers in PubMed
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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

63 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

J A Kleinschmidt
C Dingwall
G Maier
W W Franke

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the amphibian oocyte, most of the non-chromatin-bound histones are not free but form complexes with specific karyophilic proteins, the most prominent being nucleoplasmin and 'protein N1/N2'. Using antibodies against polypeptide N1 and N2 (Mr approximately 105,000 and approximately 110,000) we have isolated, from a Xenopus laevis ovary lambda gt11 expression library, several full length cDNA clones encoding one of the two closely related polypeptides N1 and N2 (these could not be distinguished by hybridization techniques). The amino acid sequence deduced from one of these clones (N1/N2, lambda 106.2) defines a polypeptide of mol. wt 64,774. The remarkably high difference between the value of Mr approximately 110,000 estimated from SDS-PAGE mobility and the true mol. wt has been found for (i) the cell protein, (ii) the polypeptide synthesized in vitro by transcription and translation and (iii) the fusion protein with beta-galactosidase expressed in Escherichia coli, indicating that the protein runs anomalously on SDS-PAGE. The amino and carboxy termini of the purified protein N1/N2 have been confirmed by direct amino acid sequencing of CNBr fragments. The amino acid sequence displays two glutamic acid-rich domains, which are probably involved in the interaction with the histones, and a putative nuclear targeting signal with high homology to that of the SV40 large T-antigen which is located near the carboxy terminus.(ABSTRACT TRUNCATED AT 250 WORDS)

Indexed as

Chromosomal Proteins, Non-HistoneCloning, MolecularNuclear ProteinsTranscription, GeneticAmino Acid SequenceAnimalsBase SequenceCarrier ProteinsDNAEscherichia coliMolecular WeightXenopusCarrier ProteinsChromosomal Proteins, Non-HistoneDNAN1-N2 protein, XenopusNuclear Proteins

Identifiers

PMID3549279
PMCPMC1167392

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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.