H
Harry F. Noller
Researcher at University of California, Santa Cruz
Publications - 252
Citations - 36077
Harry F. Noller is an academic researcher from University of California, Santa Cruz. The author has contributed to research in topics: Ribosome & Ribosomal RNA. The author has an hindex of 94, co-authored 250 publications receiving 34946 citations. Previous affiliations of Harry F. Noller include King's College London & American Cyanamid.
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Independent in vitro assembly of a ribonucleoprotein particle containing the 3' domain of 16S rRNA
TL;DR: Results show that the 3' domain of 16S rRNA can indeed assemble independently of the rest of the 30S subunit into a particle that resembles its structure in the ribosome.
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Identification of a ribosomal protein essential for peptidyl transferase activity
TL;DR: Of the 18 ribosomal proteins found in the LiC1 SP, only L16 is essential for reconstitution of peptidyl transferase activity, which can be restored to theLiC1 cores by reconstitutes with LiC 1 SP under conditions of high temperature and high ionic strength.
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Molecular mechanics of 30S subunit head rotation
TL;DR: Comparative structure analysis across 55 ribosome structures shows that 30S head movement results from flexing at two hinge points lying within conserved elements of 16S rRNA, which explains the mode of action of spectinomycin, an antibiotic that blocks translocation by binding to hinge 2.
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Accurate translocation of mRNA by the ribosome requires a peptidyl group or its analog on the tRNA moving into the 30S P site.
Kurt Fredrick,Harry F. Noller +1 more
TL;DR: This work monitors the position of mRNA within the ribosome before and after EF-G-catalyzed translocation near the initiation site, showing translocational accuracy depends on the acylation state of the tRNA entering the 30S P site.
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The ribosome in focus: new structures bring new insights
TL;DR: The structural basis of the discrimination of cognate tRNA, the high affinity for tRNA in the peptidyl-tRNA site, the structure of the peptide transferase catalytic center, the specificity of the exit site for deacylated tRNA and other functional properties of the ribosome are explained, confirmed or visualized for the first time in complexes containing full-length tRNAs and defined mRNAs.