Evidence map›Paper›PMID 1396572›Full record

ArticleThe EMBO journal1992

Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae.

S Zhang, C Lockshin, A Herbert, E Winter, A Rich

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
4.7field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

71 citing papers in PubMed, 266 citations in OpenAlex.

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  14. Tunable Protein Hydrogels: Present State and Emerging Development.Advances in biochemical engineering/biotechnology · 2021
    Article
  15. Self-assembling peptides: From a discovery in a yeast protein to diverse uses and beyond.Protein science : a publication of the Protein Society · 2020
    Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Review

11 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

S ZhangDepartment of Biology 16-739, Massachusetts Institute of Technology, Cambridge 02139.
C Lockshin
A Herbert
E Winter
A Rich
Massachusetts Institute of Technology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A putative Z-DNA binding protein, named zuotin, was purified from a yeast nuclear extract by means of a Z-DNA binding assay using [32P]poly(dG-m5dC) and [32P]oligo(dG-Br5dC)22 in the presence of B-DNA competitor. Poly(dG-Br5dC) in the Z-form competed well for the binding of a zuotin containing fraction, but salmon sperm DNA, poly(dG-dC) and poly(dA-dT) were not effective. Negatively supercoiled plasmid pUC19 did not compete, whereas an otherwise identical plasmid pUC19(CG), which contained a (dG-dC)7 segment in the Z-form was an excellent competitor. A Southwestern blot using [32P]poly(dG-m5dC) as a probe in the presence of MgCl2 identified a protein having a molecular weight of 51 kDa. The 51 kDa zuotin was partially sequenced at the N-terminal and the gene, ZUO1, was cloned, sequenced and expressed in Escherichia coli; the expressed zuotin showed similar Z-DNA binding activity, but with lower affinity than zuotin that had been partially purified from yeast. Zuotin was deduced to have a number of potential phosphorylation sites including two CDC28 (homologous to the human and Schizosaccharomyces pombe cdc2) phosphorylation sites. The hexapeptide motif KYHPDK was found in zuotin as well as in several yeast proteins, DnaJ of E.coli, csp29 and csp32 proteins of Drosophila and the small t and large T antigens of the polyoma virus. A 60 amino acid segment of zuotin has similarity to several histone H1 sequences. Disruption of ZUO1 in yeast resulted in a slow growth phenotype.

Indexed as

Saccharomyces cerevisiae ProteinsAmino Acid SequenceAnimalsBase SequenceCell NucleusChromatography, AffinityCloning, MolecularDNA-Binding ProteinsEscherichia coliFungal ProteinsGenes, FungalHumansMolecular ChaperonesMolecular Sequence DataMutagenesis, Site-DirectedNucleic Acid ConformationDNA-Binding ProteinsFungal ProteinsMolecular ChaperonesOligodeoxyribonucleotidesPolydeoxyribonucleotidesSaccharomyces cerevisiae ProteinsZUO1 protein, S cerevisiaeNASA Discipline ExobiologyNon-NASA Center

Identifiers

PMID1396572
PMCPMC556839
OpenAlexW121335872

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.