Escherichia coli 3'-terminal 16S rRNA sequence modulated fidelity during translation.
The ribosome is a central component of the protein synthetic apparatus. Although progress has been made in characterizing the functional role of many of the ribosomal proteins, the properties of ribosomal RNA and its role in ribosome structure and function are not well understood. To investigate the working properties of the highly conserved 3'-end of 16S rRNA, a site-specific deletion was made directly within the 16S rRNA molecule. The terminal deletion did not impair in vitro 30S subunit assembly, but the particles produced lost translational fidelity in an in vitro translation system primed with natural mRNA.
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Department of Biochemistry and Biophysics, Oregon State University, Corvallis 97331.
Schaup
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D001345:Autoradiography; D001483:Base Sequence; D002498:Centrifugation; D004722:Endoribonucleases / Q000378:metabolism; D004926:Escherichia coli; D009690:Nucleic Acid Conformation; D010442:Peptide Chain Initiation, Translational; D014176:Protein Biosynthesis; D012335:RNA, Ribosomal / Q000032:analysis*; D012336:RNA, Ribosomal, 16S / Q000032:analysis*; D016914:Ribonuclease H; D012269:Ribosomal Proteins / Q000032:analysis
D012335:RNA, Ribosomal; D012336:RNA, Ribosomal, 16S; D012269:Ribosomal Proteins; C040469:ribosomal protein S30; D004722:Endoribonucleases; D016914:Ribonuclease H