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. 2020 Dec 16;49(1):547–567. doi: 10.1093/nar/gkaa1195

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© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 8. — A novel ribosomal protein: bL38. (A) Sequence alignment of bL38 proteins from fifteen Bacteroidetes, three representatives of each class Flavobacteriia, Bacteroidia, Cytophagia, Sphingobacteriia, and Chitinophagia (top to bottom, species listed). (B) RNA-seq and ribo-seq read coverage across rpmB (bL28), rpmG (bL33), and rpmL (bL38) in F. johnsoniae. Ratios of average per-nucleotide coverage are 1.0:1.1:1.3 (RNA-seq) and 1.0:0.6:0.5 (ribo-seq), respectively. (C) Ribbon representation of the overall 50S subunit (side view) from F. johnsoniae, highlighting the location of the unassigned protein density with respect to uL6 (marine blue; left panel). The modeled amino acid sequence for bL38 (from Lys 14 to Lys 48) is shown fitted into the density of the cryo-EM map (right panel; top) along with a close-up view of the left panel (right panel; bottom). The close-up view shows a cartoon representation of the newly described r protein, bL38 folding into a β-hairpin that forms a mixed β-sheet with r protein uL6. It also shows its close association with helices H95 and H97 (labelled and highlighted in light blue).