A5075088228- RNA and protein synthesis mechanisms
- RNA modifications and cancer
- RNA Research and Splicing
- Cancer-related gene regulation
- Cancer-related molecular mechanisms research
- Hepatitis C virus research
- DNA and Nucleic Acid Chemistry
- Bacteriophages and microbial interactions
- HIV Research and Treatment
- Bacterial Genetics and Biotechnology
- interferon and immune responses
Uppsala University
2015-2023
University of Copenhagen
2023
When the ribosome encounters a stop codon, it recruits release factor (RF) to hydrolyze ester bond between peptide chain and tRNA. RFs have structural motifs that recognize codons in decoding center GGQ motif for induction of hydrolysis peptidyl transfer 70 Å away. Surprisingly, free RF2 is compact, with only 20 its codon-reading motifs. Cryo-EM showed ribosome-bound extended structures, suggesting are compact when entering then extend their structures upon codon recognition. Here we use...
We have studied the pH dependence of rate termination bacterial protein synthesis catalyzed by a class-1 release factor (RF1 or RF2). used classical quench-flow technique and newly developed stopped-flow that relies on use fluorescently labeled peptides. found to increase with increasing and, eventually, saturate at about 70 s(-1) an apparent pKa value 7.6. From our data, we suggest RF is limited chemistry ester bond hydrolysis low stop-codon-dependent pH-independent conformational change...
We used quench flow to study how N6-methylated adenosines (m6A) affect the accuracy ratio between kcat/Km (i.e. association rate constant (ka) times probability (Pp) of product formation after enzyme-substrate complex formation) for cognate and near-cognate substrate mRNA reading by tRNAs peptide release factors 1 2 (RFs) during translation with purified Escherichia coli components. estimated Glu-tRNAGlu, EF-Tu GTP forming ternary (T3) (GAA Gm6AA) or (GAU Gm6AU) codons. ka decreased 10-fold...
Abstract In bacteria, release of newly synthesized proteins from ribosomes during translation termination is catalyzed by class-I factors (RFs) RF1 or RF2, reading UAA and UAG UGA codons, respectively. Class-I RFs are recycled the post-termination ribosome a class-II RF, GTPase RF3, which accelerates intersubunit rotation RF dissociation. How conformational states coupled to binding dissociation remains unclear importance ribosome-catalyzed guanine nucleotide exchange on RF3 for recycling in...
Abstract When the mRNA translating ribosome encounters a stop codon in its aminoacyl site (A site), it recruits class-1 release factor (RF) to induce hydrolysis of ester bond between peptide chain and peptidyl-site (P-site) tRNA. This process, called termination translation, is under strong selection pressure for high speed accuracy. Class-1 RFs (RF1, RF2 bacteria, eRF1 eukarya aRF1 archaea), have structural motifs that recognize codons decoding center (DC) universal GGQ motif induction...