Phosphorylation of the N ‐terminal domain of ribosomal P‐stalk protein uL10 governs its association with the ribosome

AbstractThe uL10 ‐protein is the main constituent of the ribosomal‐P‐stalk, anchoring the whole stalk to the ribosome through interactions with rRNA. The P‐stalk is the core of the GTPase associated center (GAC), a critical element for ribosome biogenesis and ribosome translational activity. All P‐stalk pr oteins (uL10, P1 and P2) undergo phosphorylation within their C‐termini. Here, we show that uL10 has multiple phosphorylation sites, mapped also within the N‐terminal rRNA‐binding‐domain. Our results reveal that the introduction of a negative charge within the N‐terminus of uL10 impairs it s association with the ribosome. These findings demonstrate that uL10 N‐terminal phosphorylation has regulatory potential governing the uL10 interaction with the ribosome and may control the activity of GAC.

Source: FEBS Letters - July 14, 2020 Category: Biochemistry Authors: Kamil Filipek, Barbara Michalec ‐Wawiórka, Aleksandra Boguszewska, Sebastian Kmiecik, Marek Tchórzewski Tags: ARTICLE Source Type: research