InterPro domain: IPR035566

The ribosomal protein family L20, from the large (50S) subunit, contains members from eubacteria, as well as their mitochondrial and plastid homologs. L20 is an assembly protein, required for the first in vitro reconstitution step of the 50S ribosomal subunit, but does not seem to be essential for ribosome activity. L20 has been shown to partially unfold in the absence of RNA, in regions corresponding to the RNA-binding sites. L20 represses the translation of its own mRNA via specific binding to two distinct mRNA sites, in a manner similar to the L20 interaction with 23S ribosomal RNA [ 1 , 2 , 3 , 4 , 5 , 6 , 7 ].

This superfamily represents the C-terminal domain of the ribosomal protein L20. The C-terminal domain of this protein is an alpha-helical domain. It specifically recognizes RNA [ 8 ].

1. The role of disordered ribosomal protein extensions in the early steps of eubacterial 50 S ribosomal subunit assembly. Int J Mol Sci 10, 817-34
2. A competition mechanism regulates the translation of the Escherichia coli operon encoding ribosomal proteins L35 and L20. J. Mol. Biol. 375, 612-25
3. Escherichia coli ribosomal protein L20 binds as a single monomer to its own mRNA bearing two potential binding sites. Nucleic Acids Res. 35, 3016-31
4. Ribosomal protein L20 controls expression of the Bacillus subtilis infC operon via a transcription attenuation mechanism. Nucleic Acids Res. 35, 1578-88
5. Coexistence of two protein folding states in the crystal structure of ribosomal protein L20. EMBO Rep. 7, 1013-8
6. Double molecular mimicry in Escherichia coli: binding of ribosomal protein L20 to its two sites in mRNA is similar to its binding to 23S rRNA. Mol. Microbiol. 56, 1441-56
7. Messenger RNA secondary structure and translational coupling in the Escherichia coli operon encoding translation initiation factor IF3 and the ribosomal proteins, L35 and L20. J. Mol. Biol. 228, 366-86
8. NMR structure of bacterial ribosomal protein l20: implications for ribosome assembly and translational control. J. Mol. Biol. 323, 143-51