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Phosphorylation of the N‐terminal domain of ribosomal P‐stalk protein uL10 governs its association with the ribosome
Author(s) -
Filipek Kamil,
MichalecWawiórka Barbara,
Boguszewska Aleksandra,
Kmiecik Sebastian,
Tchórzewski Marek
Publication year - 2020
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13885
Subject(s) - ribosome , ribosome biogenesis , ribosomal protein , eukaryotic ribosome , ribosomal rna , stalk , phosphorylation , 5.8s ribosomal rna , microbiology and biotechnology , biology , translation (biology) , chemistry , biochemistry , rna , messenger rna , gene , horticulture
The 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 proteins (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 its 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.