Evidence map›Paper›PMID 9421523›Full record

ArticleNucleic acids research1998

Cys2/His2 zinc-finger protein family of petunia: evolution and general mechanism of target-sequence recognition.

K i Kubo, A Sakamoto, A Kobayashi, Z Rybka, Y Kanno, H Nakagawa, H Takatsuji

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

75 citing papers in PubMed, 160 citations in OpenAlex.

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  15. Genome-Wide Analysis ofPlants (Basel, Switzerland) · 2023
    Article
  16. International journal of molecular sciences · 2022
    Article
  17. Article
  18. Article
  19. C2H2 Zinc Finger Proteins Response to Abiotic Stress in Plants.International journal of molecular sciences · 2022
    Review
  20. PpZAT5 suppresses the expression of a B-box geneFrontiers in plant science · 2022
    Article

15 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

7 authors at 2 institutions in 1 country.

K i KuboLaboratory of Developmental Biology, National Institute of Agrobiological Resources, 2-1-2 Kannondai, Tsukuba, Ibaraki 305, Japan.
A Sakamoto
A Kobayashi
Z Rybka
Y Kanno
H Nakagawa
H Takatsuji
Institute of Agrobiological Sciences · JPTohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The EPF family is a group of Cys2/His2zinc-finger proteins in petunia. In these proteins, characteristically long spacer regions have been found to separate the zinc fingers. Our previous DNA-binding studies demonstrated that two-fingered proteins (ZPT2-1 and ZPT2-2), which have spacers of different lengths, bind to two separate AGT core motifs in a spacing specific manner. To investigate the possibility that these proteins might distinguish between the target sequences on the basis of spacing between the core motifs, we screened petunia cDNA library for other proteins belonging to this family. Initial screening by PCR and subsequent cloning of full-length cDNAs allowed us to identify the genes for 10 new proteins that had two, three or four zinc fingers. Among the two-fingered proteins the spacing between zinc fingers varied from 19 to 65 amino acids. The variation in the length of spacers was even more extensive in three- and four-fingered proteins. The presence of such proteins is consistent with our hypothesis that the spacing between the core motifs might be important for target sequence recognition. Furthermore, comparison of diverse protein structures suggests that three- and two-fingered proteins might have resulted due to successive loss of fingers from a four-fingered protein during molecular evolution. We also demonstrate that a highly conserved motif (QALGGH) among the members of EPF family and other Cys2/His2 zinc-finger proteins in plants is critical for the DNA-binding activity.

Indexed as

CysteineHistidineZinc FingersAmino Acid SequenceBinding SitesCloning, MolecularConserved SequenceDNADNA-Binding ProteinsEvolution, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPhylogenyPlant ProteinsPlantsSequence AlignmentCysteineDNADNA-Binding ProteinsHistidinePlant Proteins

Identifiers

PMID9421523
PMCPMC147284
OpenAlexW2085691784

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.