RPL22

In Toxoplasma gondii, RPL22 is a large ribosomal subunit protein whose abundance is differentially regulated relative to the small subunit protein RPS13: upon conditional knockdown of rps13, RPL22 protein levels decline more slowly than RPS13, indicating that RPL22 expression is partially buffered from small-subunit depletion (PMID:21124925). Beyond this differential-stability observation (PMID:21124925), no direct enzymatic, structural, or binding-partner mechanism for RPL22 has been characterized in the available corpus.

1. 2010 Medium

   It was unknown whether large- and small-subunit ribosomal protein levels are co-regulated; measuring RPL22 during RPS13 depletion showed that RPL22 decays more slowly, establishing that ribosomal protein abundance is differentially buffered across subunits.

   Evidence Conditional tetracycline-repressor knockdown of rps13 with Myc-tagged RPL22 protein quantitation in Toxoplasma gondii

   PMID:21124925

   Open questions at the time

   • No mechanism for the differential stability of RPL22 versus RPS13 is defined
   • No direct enzymatic, structural, or binding-partner activity for RPL22 established
   • RPL22 was a secondary observation in a study focused on RPS13

• The molecular function, ribosome incorporation, and any regulatory or extra-ribosomal role of Toxoplasma RPL22 remain uncharacterized.
• No structural or biochemical characterization of RPL22 within the ribosome
• No binding partners or substrates identified
• Mechanism underlying differential buffering versus RPS13 unknown