PropertyValue
?:abstract
  • 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.
?:creator
?:journal
  • FEBS_lett
?:license
  • unk
?:publication_isRelatedTo_Disease
?:source
  • WHO
?:title
  • Phosphorylation of the N-terminal domain of ribosomal P-stalk protein uL10 governs its association with the ribosome
?:type
?:who_covidence_id
  • #32668052
?:year
  • 2020

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