Human ribosomal protein L7 displays an ER binding property and is involved in ribosome‐ER association

This is the authors' abstract. We don't add key points for this paper.

Human ribosomal protein L7 incorporates an ER-binding characteristic. It is evident from the in vivo ER co-localization of the transiently expressed recombinant L7 in mycophenolic acid treated HeLa cells, the in situ detection of the fluorescent L7 at the ER in digitonin-permeablized HeLa cells, and the expression of a similar K(D) value to ribosomes binding to the ER. However, no ER co-localization and a lower K(D) was observed if the last 50 amino acid residues at the carboxyl end of L7 were removed, implying that the carboxyl region embodies the ER-binding specificity. Based on the inhibitory effect of an anti L7 antibody during ribosome rebinding to the microsome, we suggest that the L7-ER-binding nature could be one of multiple factors that allow a nascent peptide-less ribosome to remain at the ER.