ArticleG3 (Bethesda, Md.)2015
GFP Loss-of-Function Mutations in Arabidopsis thaliana.
Article in G3 (Bethesda, Md.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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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.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Development of multiplexed orthogonal base editor (MOBE) systems.Nature biotechnology · 2025Article
- Engineered mischarged transfer RNAs for correcting pathogenic missense mutations.Molecular therapy : the journal of the American Society of Gene Therapy · 2024Article
- A GFP splicing reporter in a coilin mutant background reveals links between alternative splicing, siRNAs, and coilin function in Arabidopsis thaliana.G3 (Bethesda, Md.) · 2023Article
- The Wild-Type tRNA Adenosine Deaminase Enzyme TadA Is Capable of Sequence-Specific DNA Base Editing.Chembiochem : a European journal of chemical biology · 2023Article
- Curing "GFP-itis" in Bacteria with Base Editors: Development of a Genome Editing Science Program Implemented with High School Biology Students.The CRISPR journal · 2023Article
- Curing "GFP-itis" in Bacteria with Base Editors: Development of a Genome Editing Science Program Implemented with High School Biology Students.bioRxiv : the preprint server for biology · 2023Article
- Article
- Precise in vivo functional analysis of DNA variants with base editing using ACEofBASEs target prediction.eLife · 2022Article
- A Collection of Pre-mRNA Splicing Mutants inG3 (Bethesda, Md.) · 2020Article
- CRISPR-TSKO: A Technique for Efficient Mutagenesis in Specific Cell Types, Tissues, or Organs in Arabidopsis.The Plant cell · 2019Article
- Article
- PRP4KA, a Putative Spliceosomal Protein Kinase, Is Important for Alternative Splicing and Development inGenetics · 2018Article
- A Rapid and Precise Mutation-Activated Fluorescence Reporter for Analyzing Acute Mutagenesis Frequency.Cell chemical biology · 2018Article
- A Genetic Screen Identifies PRP18a, a Putative Second Step Splicing Factor Important for Alternative Splicing and a Normal Phenotype inG3 (Bethesda, Md.) · 2018Article
- A Genetic Screen for Pre-mRNA Splicing Mutants ofGenetics · 2017Article
- A genetic screen implicates a CWC16/Yju2/CCDC130 protein and SMU1 in alternative splicing inRNA (New York, N.Y.) · 2017Article
- A novel twelve class fluctuation test reveals higher than expected mutation rates for influenza A viruses.eLife · 2017Article
- Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Green fluorescent protein (GFP) and related fluorescent proteins are widely used in biological research to monitor gene expression and protein localization in living cells. The GFP chromophore is generated spontaneously in the presence of oxygen by a multi-step reaction involving cyclization of the internal tripeptide Ser65 (or Thr65)-Tyr66-Gly67, which is embedded in the center of an 11-stranded β-barrel structure. Random and site-specific mutagenesis has been used to optimize GFP fluorescence and create derivatives with novel properties. However, loss-of-function mutations that would aid in understanding GFP protein folding and chromophore formation have not been fully cataloged. Here we report a collection of ethyl methansulfonate-induced GFP loss-of-function mutations in the model plant Arabidopsis thaliana. Mutations that alter residues important for chromophore maturation, such as Arg96 and Ser205, greatly reduce or extinguish fluorescence without dramatically altering GFP protein accumulation. By contrast, other loss-of-fluorescence mutations substantially diminish the amount of GFP protein, suggesting that they compromise protein stability. Many mutations in this category generate substitutions of highly conserved glycine residues, including the following: Gly67 in the chromogenic tripeptide; Gly31, Gly33, and Gly35 in the second β-strand; and Gly20, Gly91, and Gly127 in the lids of the β-barrel scaffold. Our genetic analysis supports conclusions from structural and biochemical studies and demonstrates a critical role for multiple, highly conserved glycine residues in GFP protein stability.
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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.