| Property | Value |
|---|
|
?: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.
|
|
is
?:annotates
of
|
|
|
?:creator
|
|
|
?:doi
|
|
|
?:doi
|
|
|
?:journal
|
|
|
?:license
|
|
|
?:pmid
|
|
|
?:pmid
|
|
|
?:publication_isRelatedTo_Disease
|
|
|
?:source
|
|
|
?:title
|
-
Phosphorylation of the N-terminal domain of ribosomal P-stalk protein uL10 governs its association with the ribosome.
|
|
?:type
|
|
|
?:year
|
|
![[This page as RDF]](https://research.tib.eu/covid-19/static/rdf-icon.gif){kind=icon}