ArticlePlant physiology2011
Interaction of the tobacco lectin with histone proteins.
Article in Plant physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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.
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.
Who cites it
24 citing papers in PubMed, 54 citations in OpenAlex.
- The crystal structure of Nictaba reveals its carbohydrate-binding properties and a new lectin dimerization mode.Glycobiology · 2024Article
- O-GlcNAcylation: the sweet side of epigenetics.Epigenetics & chromatin · 2023Review
- 35 years in plant lectin research: a journey from basic science to applications in agriculture and medicine.Glycoconjugate journal · 2022Article
- 130 years of Plant Lectin Research.Glycoconjugate journal · 2020Review
- OsEUL Lectin Gene Expression in Rice: Stress Regulation, Subcellular Localization and Tissue Specificity.Frontiers in plant science · 2020Article
- Review
- An Arabidopsis TIR-Lectin Two-Domain Protein Confers Defense Properties againstPlant physiology · 2019Article
- Critical observations that shaped our understanding of the function(s) of intracellular glycosylation (O-GlcNAc).FEBS letters · 2018Review
- Proteomic analysis of the OGT interactome: novel links to epithelial-mesenchymal transition and metastasis of cervical cancer.Carcinogenesis · 2018Article
- Article
- Phosphorylation coexists with O-GlcNAcylation in a plant virus protein and influences viral infection.Molecular plant pathology · 2018Article
- H2A O-GlcNAcylation at serine 40 functions genomic protection in association with acetylated H2AZ or γH2AX.Epigenetics & chromatin · 2017Article
- Nictaba Homologs fromFrontiers in plant science · 2017Article
- The lectin-like protein 1 in Lactobacillus rhamnosus GR-1 mediates tissue-specific adherence to vaginal epithelium and inhibits urogenital pathogens.Scientific reports · 2016Article
- Physiology and molecular biology of plants : an international journal of functional plant biology · 2016Article
- The Putative O-Linked N-Acetylglucosamine Transferase SPINDLY Inhibits Class I TCP Proteolysis to Promote Sensitivity to Cytokinin.Plant physiology · 2016Article
- Overexpression ofFrontiers in plant science · 2016Article
- Review
- Protein-carbohydrate interactions as part of plant defense and animal immunity.Molecules (Basel, Switzerland) · 2015Review
- HIV-1 and its resistance to peptidic carbohydrate-binding agents (CBAs): an overview.Molecules (Basel, Switzerland) · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells. Since tobacco lectin expression is only observed after the plant has been subjected to stress situations such as jasmonate treatment or insect attack, Nictaba is believed to act as a signaling protein involved in the stress physiology of the plant. In this paper, a nuclear proteomics approach was followed to identify the binding partners for Nictaba in the nucleus and the cytoplasm of tobacco cv Xanthi cells. Using lectin affinity chromatography and pull-down assays, it was shown that Nictaba interacts primarily with histone proteins. Binding of Nictaba with histone H2B was confirmed in vitro using affinity chromatography of purified calf thymus histone proteins on a Nictaba column. Elution of Nictaba-interacting histone proteins was achieved with 1 m N-acetylglucosamine (GlcNAc). Moreover, mass spectrometry analyses indicated that the Nictaba-interacting histone proteins are modified by O-GlcNAc. Since the lectin-histone interaction was shown to be carbohydrate dependent, it is proposed that Nictaba might fulfill a signaling role in response to stress by interacting with O-GlcNAcylated proteins in the plant cell nucleus.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.