Structural analysis of noncanonical translation initiation complexes.

ABSTRACT: Translation initiation is a highly regulated, multi-step process that is critical for efficient and accurate protein synthesis. In bacteria, initiation begins when mRNA, initiation factors, and a dedicated initiator fMet-tRNA^fMet bind the small (30S) ribosomal subunit. Specific binding of fMet-tRNA^fMet in the peptidyl (P) site is mediated by the inspection of the fMet moiety by initiation factor IF2 and of three conserved G-C base pairs in the tRNA anticodon stem by the 30S head domain. Tandem A-minor interactions form between 16S ribosomal RNA nucleotides A1339 and G1338 and tRNA base pairs G30-C40 and G29-C41, respectively. Swapping the G30-C40 pair of tRNA^fMet with C-G (called tRNA^fMet M1) reduces discrimination against the noncanonical start

SUBMITTER: Mattingly JM 

PROVIDER: S-EPMC11497404 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature