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The sarcin-ricin loop (SRL) is one of the most conserved segments of ribosomal RNA (rRNA). Translational GTPases (trGTPases), such as EF-G and EF-Tu and IF2, form contacts with the SRL that are critical for GTP hydrolysis and factor function. Previous studies showed that expression of 23S rRNA lacking the SRL confers a dominant lethal phenotype in E.
View Article and Find Full Text PDFDynamic binding of the bacterial chaperone Trigger factor to translating ribosomes in .
Proc Natl Acad Sci U S A
January 2025
Department of Cell & Molecular Biology, Uppsala University, Uppsala SE-75124, Sweden.
The bacterial chaperone Trigger factor (TF) binds to ribosome-nascent chain complexes (RNCs) and cotranslationally aids the folding of proteins in bacteria. Decades of studies have given a broad, but often conflicting, description of the substrate specificity of TF, its RNC-binding dynamics, and competition with other RNC-binding factors, such as the Signal Recognition Particle (SRP). Previous RNC-binding kinetics experiments were commonly conducted on stalled RNCs in reconstituted systems, and consequently, may not be representative of the interaction of TF with ribosomes translating mRNA in the cytoplasm of the cell.
View Article and Find Full Text PDFBiosynthesis of Bacteriochlorophylls and Bacteriochlorophyllides in Escherichia coli.
Biotechnol Bioeng
December 2024
Department of Microbiology, Hubei Key Laboratory of Cell Homeostasis, College of Life Science, TaiKang Center for Life and Medical Sciences, Wuhan University, Wuhan, China.
Photosynthesis, the most important biological process on Earth, converts light energy into chemical energy with essential pigments like chlorophylls and bacteriochlorophylls. The ability to reconstruct photosynthesis in heterotrophic organisms could significantly impact solar energy utilization and biomass production. In this study, we focused on constructing light-dependent biosynthesis pathways for bacteriochlorophyll (BChl) a and bacteriochlorophyllide (BChlide) d and c in the model strain Escherichia coli.
View Article and Find Full Text PDFTracking transcription-translation coupling in real time.
Nature
January 2025
Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.
Article Synopsis
- Researchers are investigating how macromolecular machines in bacteria, specifically ribosomes and RNA polymerase (RNAP), work together during transcription and translation within the same cellular space.
- High-resolution structures have given some insights, but there’s a lack of understanding of these mechanisms in a dynamic setting.
- Using advanced fluorescence microscopy, the study reveals that ribosome and RNAP can effectively cooperate over long distances through mRNA looping, influenced by NusG, showcasing how this physical interaction optimizes gene expression despite challenges like RNAP pausing.
Expanding the Substrate Selectivity of the Fimsbactin Biosynthetic Adenylation Domain, FbsH.
ACS Chem Biol
December 2024
Department of Structural Biology, University at Buffalo, Buffalo, New York 14203, United States.
Nonribosomal peptide synthetases (NRPSs) produce diverse natural products including siderophores, chelating agents that many pathogenic bacteria produce to survive in low iron conditions. Engineering NRPSs to produce diverse siderophore analogs could lead to the generation of novel antibiotics and imaging agents that take advantage of this unique iron uptake system in bacteria. The highly pathogenic and antibiotic-resistant bacteria produces fimsbactin, an unusual branched siderophore with iron-binding catechol groups bound to a serine or threonine side chain.
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