Evidence map›Paper›PMID 17028207›Full record

ArticleThe Plant cell2006

Identification and characterization of components of a putative petunia S-locus F-box-containing E3 ligase complex involved in S-RNase-based self-incompatibility.

Zhihua Hua, Teh-Hui Kao

Abstract read
In one paragraph

Article in The Plant cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
–field-weighted citation impact
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

80 citing papers in PubMed.

  1. Genome-wide identification and analysis ofFrontiers in plant science · 2026
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  13. Downregulated expression of SHorticulture research · 2021
    Article
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  15. Trans-acting regulators of ribonuclease activity.Journal of microbiology (Seoul, Korea) · 2021
    Review
  16. Article
  17. Functional Analyses of Flavonol Synthase Genes FromFrontiers in plant science · 2021
    Article
  18. Review
  19. Article
  20. Article

20 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

2 authors.

Zhihua HuaIntercollege Graduate Degree Program in Plant Biology, Pensylvania State University, University Park, Pensylvania 16802, USA.
Teh-Hui Kao

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Petunia inflata S-locus F-box (Pi SLF) is thought to function as a typical F-box protein in ubiquitin-mediated protein degradation and, along with Skp1, Cullin-1, and Rbx1, could compose an SCF complex mediating the degradation of nonself S-RNase but not self S-RNase. We isolated three P. inflata Skp1s (Pi SK1, -2, and -3), two Cullin-1s (Pi CUL1-C and -G), and an Rbx1 (Pi RBX1) cDNAs and found that Pi CUL1-G did not interact with Pi RBX1 and that none of the three Pi SKs interacted with Pi SLF(2). We also isolated a RING-HC protein, S-RNase Binding Protein1 (Pi SBP1), almost identical to Petunia hybrida SBP1, which interacts with Pi SLFs, S-RNases, Pi CUL1-G, and an E2 ubiquitin-conjugating enzyme, suggesting that Pi CUL1-G, SBP1, and SLF may be components of a novel E3 ligase complex, with Pi SBP1 playing the roles of Skp1 and Rbx1. S-RNases interact more with nonself Pi SLFs than with self Pi SLFs, and Pi SLFs also interact more with nonself S-RNases than with self S-RNases. Bacterially expressed S(1)-, S(2)-, and S(3)-RNases are degraded by the 26S proteasomal pathway in a cell-free system, albeit not in an S-allele-specific manner. Native glycosylated S(3)-RNase is not degraded to any significant extent; however, deglycosylated S(3)-RNase is degraded as efficiently as the bacterially expressed S-RNases. Finally, S-RNases are ubiquitinated in pollen tube extracts, but whether this is mediated by the Pi SLF-containing E3 complex is unknown.

Indexed as

Molecular Sequence DataPetuniaRibonucleasesSKP Cullin F-Box Protein LigasesTwo-Hybrid System TechniquesUbiquitin-Protein LigasesRibonucleasesSKP Cullin F-Box Protein LigasesUbiquitin-Protein Ligases

Identifiers

PMID17028207
PMCPMC1626602

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.