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The pseudouridylase Pus1 catalyzes pseudouridine (Ψ) formation at multiple uridine residues in tRNAs, and in some snRNAs and mRNAs. Although Pus1 is highly conserved, and mutations are associated with human disease, little is known about eukaryotic Pus1 biology. Here, we show that Schizosaccharomyces pombe pus1Δ mutants are temperature sensitive due to decay of tRNAIle(UAU), as tRNAIle(UAU) levels are reduced, and its overexpression suppresses the defect.
View Article and Find Full Text PDFScreening a library of temperature-sensitive mutants to identify secretion factors in .
J Bacteriol
January 2025
Department of Microbiology, Howard Taylor Ricketts Laboratory, The University of Chicago, Chicago, Illinois, USA.
Protein secretion is an essential cell process in bacteria, required for cell envelope biogenesis, export of virulence factors, and acquisition of nutrients, among other important functions. In the Sec secretion pathway, signal peptide-bearing precursors are recognized by the SecA ATPase and pushed across the membrane through a translocon channel made of the proteins SecY, SecE, and SecG. The Sec pathway has been extensively studied in the model organism , but the Sec pathways of other bacteria such as the human pathogen differ in important ways from this model.
View Article and Find Full Text PDFSystematic characterization of indel variants using a yeast-based protein folding sensor.
Structure
December 2024
Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen, Denmark. Electronic address:
Gene variants resulting in insertions or deletions of amino acid residues (indels) have important consequences for evolution and are often linked to disease, yet, compared to missense variants, the effects of indels are poorly understood and predicted. We developed a sensitive protein folding sensor based on the complementation of uracil auxotrophy in yeast by circular permutated orotate phosphoribosyltransferase (CPOP). The sensor reports on the folding of disease-linked missense variants and de-novo-designed proteins.
View Article and Find Full Text PDFTemperature-driven changes in membrane fluidity differentially impact FILAMENTATION TEMPERATURE-SENSITIVE H2-mediated photosystem II repair.
Plant Cell
December 2024
Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences (CEMPS), Chinese Academy of Sciences, Shanghai 200032, China.
Article Synopsis
- The Arabidopsis var2 mutant, which lacks functional FtsH2, is key for studying the repair process of photosystem II (PSII) in plants.
- Under cold stress, var2 mutants struggle due to increased membrane viscosity, highlighting the essential need for FtsH2's substrate extraction activity to manage this condition.
- In contrast, during heat stress, the mutant behaves like normal plants, as increased membrane fluidity allows other FtsH isomers to compensate for the lack of FtsH2, indicating that membrane fluidity significantly affects the function of the FtsH complex under various stress conditions.
Genetic and molecular studies of fitC4 and its suppressors fitA76* and fit95 in Escherichia coli.
Int Microbiol
December 2024
Department of Molecular Biology, School of Biological Sciences, Madurai Kamaraj University, Madurai, 625 021, India.
The fitA/pheS and fitB/pheT genes were previously proposed to function as transcription factors. The originally identified temperature sensitive (Ts) transcription-defective fitA76 mutant was shown to harbour a second mutation, fit95 (pheT) in addition to pheS5 (pheS; G → A transition). A new fit mutation namely, fitC4 (fitC locus) was identified in a Ts derivative of fitA76, namely JV4.
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