Daniel Larsson

Abstract Frameshifts can be caused by specific combinations of tRNA and mRNA. The wildtype AGC-decoding E. coli tRNASer3GCU has been shown to induce −1 ribosomal frameshifting on GCA alanine codons, and proposed to read a two-base codon instead of a canonical triplet. However, it has remained unclear whether this type of non-cognate decoding can be accommodated by the ribosome. Here, we perform single-particle cryo-EM reconstructions on E.

Skip navigation Like what you’re reading? Available in English 简体中文 6G standardization has reached a new milestone with the launch of technical studies in 3GPP. Moving forward from the phase of defining use cases and requirements, the focus is now on shaping the technologies that will be part of 6G. This blog post explains the key topics that will be covered and shares our views on the most important aspects.

Abstract The antibiotic resistance protein FusB rescues protein synthesis from inhibition by fusidic acid (FA), which locks elongation factor G (EF-G) to the ribosome after GTP hydrolysis. Here, we present time-resolved single–particle cryo-EM structures explaining the mechanism of FusB-mediated rescue. FusB binds to the FA-trapped EF-G on the ribosome, causing large-scale conformational changes of EF-G that break interactions with the ribosome, tRNA, and mRNA.