ArticleNucleic acids research2020
Frame-shifted proteins of a given gene retain the same function.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers, 1 of them a synthesis that pooled it.
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Who cites it
10 citing papers in PubMed, 1 synthesis or guideline pooled it, 17 citations in OpenAlex.
- Crohn's-like Enteritis in X-Linked Agammaglobulinemia: A Case Series and Systematic Review.The journal of allergy and clinical immunology. In practice · 2021Pooled it
- Effect of a truncated mutant factor V on hemostatic function and embryonic development in mice.Scientific reports · 2026Article
- Frameshift mutations in theAntimicrobial agents and chemotherapy · 2024Article
- Bedaquiline- and clofazimine- selected Mycobacterium tuberculosis mutants: further insights on resistance driven largely by Rv0678.Scientific reports · 2023Article
- Charged Amino Acids Contribute to ZorO Toxicity.Toxins · 2022Article
- Functional Attenuation of UCP1 as the Potential Mechanism for a Thickened Blubber Layer in Cetaceans.Molecular biology and evolution · 2022Article
- Frameshift and wild-type proteins are often highly similar because the genetic code and genomes were optimized for frameshift tolerance.BMC genomics · 2022Article
- Genotype to Phenotype: CRISPR Gene Editing Reveals Genetic Compensation as a Mechanism for Phenotypic Disjunction of Morphants and Mutants.International journal of molecular sciences · 2021Review
- Amplification of potential thermogenetic mechanisms in cetacean brains compared to artiodactyl brains.Scientific reports · 2021Article
- Frame-shifted proteins of a given gene are unlikely to retain the same function.RNA (New York, N.Y.) · 2020Article
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Frameshift mutations are generally considered to be lethal because it could result in radical changes of the protein sequence behind. However, the protein of frameshift mutants of a type I toxin (ibsc) was found to be still toxic to bacteria, retaining the similar function as wild-type protein to arrest the cellular growth by impairing the membrane's integrity. Additionally, we have verified that this observation is not an individual event as the same phenomenon had been found in other toxins subsequently. After analyzing the coding sequence of these genes, we proposed a hypothesis to search this kind of hidden gene, through which a dihydrofolate reductase-encoding gene (dfrB3) was found out. Like the wild-type reductase, both +1 and -1 frame-shifted proteins of dfrB3 gene were also proved to catalyze the reduction of dihydrofolate to tetrahydrofolate by using NADPH.
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