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IPR035566

Ribosomal protein bL20, C-terminal

InterPro entry
Short nameRibosomal_protein_bL20_C
Overlapping entries
 

Description

This superfamily represents the C-terminal domain of the ribosomal protein bL20. The C-terminal domain of this protein is an α-helical domain. It specifically recognizes RNA
[8]
.

This entry represents the large ribosomal subunit protein family bL20 that contains members from eubacteria, as well as their mitochondrial and plastid homologs. bL20 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. bL20 has been shown to partially unfold in the absence of RNA, in regions corresponding to the RNA-binding sites. bL20 represses the translation of its own mRNA via specific binding to two distinct mRNA sites, in a manner similar to the bL20 interaction with 23S ribosomal RNA
[7, 3, 4, 5, 6, 1, 2]
.

References

1.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. Guillier M, Allemand F, Dardel F, Royer CA, Springer M, Chiaruttini C. Mol. Microbiol. 56, 1441-56, (2005). View articlePMID: 15916597

2.Messenger RNA secondary structure and translational coupling in the Escherichia coli operon encoding translation initiation factor IF3 and the ribosomal proteins, L35 and L20. Lesage P, Chiaruttini C, Graffe M, Dondon J, Milet M, Springer M. J. Mol. Biol. 228, 366-86, (1992). View articlePMID: 1453449

3.A competition mechanism regulates the translation of the Escherichia coli operon encoding ribosomal proteins L35 and L20. Haentjens-Sitri J, Allemand F, Springer M, Chiaruttini C. J. Mol. Biol. 375, 612-25, (2008). View articlePMID: 18037435

4.Escherichia coli ribosomal protein L20 binds as a single monomer to its own mRNA bearing two potential binding sites. Allemand F, Haentjens J, Chiaruttini C, Royer C, Springer M. Nucleic Acids Res. 35, 3016-31, (2007). View articlePMID: 17439971

5.Ribosomal protein L20 controls expression of the Bacillus subtilis infC operon via a transcription attenuation mechanism. Choonee N, Even S, Zig L, Putzer H. Nucleic Acids Res. 35, 1578-88, (2007). View articlePMID: 17289755

6.Coexistence of two protein folding states in the crystal structure of ribosomal protein L20. Timsit Y, Allemand F, Chiaruttini C, Springer M. EMBO Rep. 7, 1013-8, (2006). View articlePMID: 16977336

7.The role of disordered ribosomal protein extensions in the early steps of eubacterial 50 S ribosomal subunit assembly. Timsit Y, Acosta Z, Allemand F, Chiaruttini C, Springer M. Int J Mol Sci 10, 817-34, (2009). View articlePMID: 19399222

8.NMR structure of bacterial ribosomal protein l20: implications for ribosome assembly and translational control. Raibaud S, Lebars I, Guillier M, Chiaruttini C, Bontems F, Rak A, Garber M, Allemand F, Springer M, Dardel F. J. Mol. Biol. 323, 143-51, (2002). View articlePMID: 12368106

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