scholarly journals Creation of a functional S -nitrosylation site in vitro by single point mutation

FEBS Letters ◽  
1999 ◽  
Vol 459 (3) ◽  
pp. 319-322 ◽  
Author(s):  
Carmen Castro ◽  
Félix A. Ruiz ◽  
Isabel Pérez-Mato ◽  
Manuel M. Sánchez del Pino ◽  
Leighton LeGros ◽  
...  
Keyword(s):  
Point Mutation ◽  
Single Point ◽  
Single Point Mutation

scholarly journals Impaired Infectivity of HIV-1 after a Single Point Mutation in the POL Gene to Escape the Effect of a Protease Inhibitor in Vitro

Virology ◽  
1995 ◽  
Vol 210 (1) ◽  
pp. 212-216 ◽  
Author(s):  
Marcelo J. Kuroda ◽  
Mohamed A. El-Farrash ◽  
Suranjana Choudhury ◽  
Shinji Harada
Keyword(s):  
Protease Inhibitor ◽  
Point Mutation ◽  
Single Point ◽  
Single Point Mutation ◽  
Hiv 1

scholarly journals A single point mutation in the Plasmodium falciparum ftsh1 metalloprotease confers actinonin resistance

2020 ◽  
Author(s):  
Christopher D Goodman ◽  
Taher Uddin ◽  
Natalie J Spillman ◽  
Geoffrey I McFadden
Keyword(s):  
Plasmodium Falciparum ◽  
Point Mutation ◽  
Single Point ◽  
Single Point Mutation ◽  
Post Translational Modification ◽  
Malaria Parasites ◽  
Specific Sequence ◽  
Allelic Replacement ◽  
Related Parasite

AbstractThe antibiotic actinonin kills malaria parasites (Plasmodium falciparum) by interfering with apicoplast function. Early evidence suggested that actinonin inhibited prokaryote-like post-translational modification in the apicoplast; mimicking its activity against bacteria. However, Amberg Johnson et al. (2017) identified the metalloprotease TgFtsH1 as the target of actinonin in the related parasite Toxoplasma gondii and implicated actinonin in the inhibition of P. falciparum growth. The authors were not, however, able to recover actinonin resistant malaria parasites, leaving the specific target of actinonin uncertain. We generated actinonin resistant P. falciparum by in vitro selection and identified a specific sequence change in PfftsH1 associated with resistance. Re-Introduction of this point mutation using CRISPr-Cas9 allelic replacement was sufficient to confer actinonin resistance in P. falciparum. Our data unequivocally identifies PfFtsH1 as the target of actinonin and suggests that actinonin should not be included in the highly valuable collection of “irresistible” drugs for combatting malaria.

scholarly journals Single Point Mutation from E22-to-K in Aβ Initiates Early-Onset Alzheimer’s Disease by Binding with Catalase

2020 ◽  
Vol 2020 ◽  
pp. 1-21
Author(s):  
Wenjing Jiang ◽  
YanYu ◽  
Dandan Yao ◽  
Xuechao Fei ◽  
Li Ai ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Point Mutation ◽  
Early Onset ◽  
Late Onset ◽  
Single Point ◽  
Single Point Mutation ◽  
Neuron Death ◽  
Mutation Site

Amyloid-beta (Aβ) is a critical etiological factor for late-onset familial Alzheimer’s disease (AD). However, an early-onset AD has been found to be related with an Aβ mutation in glutamic acid 22-to-lysine (Italian type E22K). Why only one single point mutation at E22 residue induces AD remains unclear. Here, we report that a Chinese familial AD pedigree with E22K mutation was associated with higher levels of serum hydrogen peroxide (H2O2) and lower activity of catalase (a H2O2 degrading enzyme) than controls. Further, we found that E22K binding with catalase caused more severe H2O2 accumulation in the brains of E22K-injected rats than Aβ-injected rats. Unexpectedly, H2O2 bound with the mutation site 22K residue of E22K and elicited more rapid aggregation of E22K than Aβ in vitro. Moreover, H2O2 acted with E22K synergistically to induce higher cellular toxicity than with Aβ. Notably, intrahippocampal infusion of E22K led to more severe plaque deposition, neuron death, and more rapid memory decline than Aβ-injected rats. However, L-cysteine, a H2O2 scavenger, not only prevented self-aggregation of E22K but also reduced H2O2-promoted E22K assembly in vitro; subsequently, it alleviated Alzheimer-related phenotypes. Hence, E22K binding with catalase promotes the early onset of familial AD, and L-cys may reverse this disease.

scholarly journals A single point mutation in the Plasmodium falciparum FtsH1 metalloprotease confers actinonin resistance

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Christopher D Goodman ◽  
Taher Uddin ◽  
Natalie J Spillman ◽  
Geoffrey I McFadden
Keyword(s):  
Plasmodium Falciparum ◽  
Point Mutation ◽  
In Vitro Selection ◽  
Single Point ◽  
Single Point Mutation ◽  
Post Translational Modification ◽  
Malaria Parasites ◽  
Specific Sequence ◽  
Allelic Replacement

The antibiotic actinonin kills malaria parasites (Plasmodium falciparum) by interfering with apicoplast function. Early evidence suggested that actinonin inhibited prokaryote-like post-translational modification in the apicoplast; mimicking its activity against bacteria. However, Amberg Johnson et al. (2017) identified the metalloprotease TgFtsH1 as the target of actinonin in the related parasite Toxoplasma gondii and implicated P. falciparum FtsH1 as a likely target in malaria parasites. The authors were not, however, able to recover actinonin resistant malaria parasites, leaving the specific target of actinonin uncertain. We generated actinonin resistant P. falciparum by in vitro selection and identified a specific sequence change in PfFtsH1 associated with resistance. Introduction of this point mutation using CRISPr-Cas9 allelic replacement was sufficient to confer actinonin resistance in P. falciparum. Our data unequivocally identify PfFtsH1 as the target of actinonin and suggests that actinonin should not be included in the highly valuable collection of ‘irresistible’ drugs for combatting malaria.

scholarly journals A single point mutation converts a proton-pumping rhodopsin into a red-shifted, turn-on fluorescent sensor for chloride

2021 ◽  
Author(s):  
Jasmine N. Tutol ◽  
Jessica Lee ◽  
Hsichuan Chi ◽  
Farah N. Faizuddin ◽  
Sameera S. Abeyrathna ◽  
...  
Keyword(s):  
Point Mutation ◽  
Fluorescent Sensor ◽  
Single Point ◽  
Proton Pumping ◽  
Single Point Mutation ◽  
Turn On ◽  
Gloeobacter Violaceus

By utilizing laboratory-guided evolution, we have converted the fluorescent proton-pumping rhodopsin GR from Gloeobacter violaceus into GR1, a red-shifted, turn-on fluorescent sensor for chloride.

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