Ribosome Elongation Kinetics of Consecutively Charged Residues Are Coupled to Electrostatic Force.

ABSTRACT: The speed of protein synthesis can dramatically change when consecutively charged residues are incorporated into an elongating nascent protein by the ribosome. The molecular origins of this class of allosteric coupling remain unknown. We demonstrate, using multiscale simulations, that positively charged residues generate large forces that move the P-site amino acid away from the A-site amino acid. Negatively charged residues generate forces of similar magnitude but move the A- and P-sites closer together. These conformational changes, respectively, increase and decrease the transition state barrier height to peptide bond formation, explaining how charged residues mechanochemically alter translation speed. This mechanochemical mechanism is consistent with in vivo ribosome profiling d

SUBMITTER: Leininger SE 

PROVIDER: S-EPMC8916236 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature