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

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.