F
IPR000911

Ribosomal protein uL11

InterPro entry
Short nameRibosomal_uL11
Overlapping
homologous
superfamilies
 
family relationships

Description

Ribosomal protein uL11, together with proteins L10 and L7/L12, and 23S rRNA, form the L7/L12 stalk on the surface of the large subunit of the ribosome. The homologous eukaryotic cytoplasmic protein uL11 was called in the past 60S ribosomal protein L12, which is distinct from the L12 involved in the formation of the L7/L12 stalk. The C-terminal domain (CTD) of uL11 is essential for binding 23S rRNA, while the N-terminal domain (NTD) contains the binding site for the antibiotics thiostrepton and micrococcin. uL11 and 23S rRNA form an essential part of the GTPase-associated region (GAR). Based on differences in the relative positions of the uL11 NTD and CTD during the translational cycle, uL11 is proposed to play a significant role in the binding of initiation factors, elongation factors, and release factors to the ribosome. Several factors, including the class I release factors RF1 and RF2, are known to interact directly with uL11. In eukaryotes, uL11 has been implicated in regulating the levels of ubiquinated p53 and MDM2 in the MDM2-p53 feedback loop, which is responsible for apoptosis in response to DNA damage. In bacteria, the "stringent response" to harsh conditions allows bacteria to survive, and ribosomes that lack uL11 are deficient in stringent factor stimulation
[2, 3, 13, 4, 5, 12, 9, 7, 10, 8, 11, 6]
.

Ribosomal protein uL11 (also known as L12 in mammals and yeast) is one of the proteins from the large ribosomal subunit. In Escherichia coli, uL11 is known to bind directly to the 23S rRNA and plays a significant role during initiation, elongation, and termination of protein synthesis. It belongs to a family of ribosomal proteins which, on the basis of sequence similarities
[1]
, groups bacteria, plant chloroplast, red algal chloroplast, cyanelle and archaeabacterial uL11; and mammalian, plant and yeast L12 (YL15). uL11 is a protein of 140 to 165 amino-acid residues and consists of a 23S rRNA binding C-terminal domain and an N-terminal domain that directly contacts protein synthesis factors. These two domains are joined by a flexible linker that allows inter-domain movement during protein synthesis. While the C-terminal domain of uL11 binds RNA tightly, the N-terminal domain makes only limited contacts with RNA and is proposed to function as a switch that reversibly associates with an adjacent region of RNA
[13, 6, 16, 15]
. In E. coli, the C-terminal half of uL11 has been shown
[14]
to be in an extended and loosely folded conformation and is likely to be buried within the ribosomal structure.

References

1.The 26S rRNA binding ribosomal protein equivalent to bacterial protein L11 is encoded by unspliced duplicated genes in Saccharomyces cerevisiae. Pucciarelli MG, Remacha M, Vilella MD, Ballesta JP. Nucleic Acids Res. 18, 4409-16, (1990). View articlePMID: 2167467

2.Structural basis for contrasting activities of ribosome binding thiazole antibiotics. Lentzen G, Klinck R, Matassova N, Aboul-ela F, Murchie AI. Chem. Biol. 10, 769-78, (2003). View articlePMID: 12954336

3.The flexible N-terminal domain of ribosomal protein L11 from Escherichia coli is necessary for the activation of stringent factor. Jenvert RM, Schiavone LH. J. Mol. Biol. 365, 764-72, (2007). View articlePMID: 17095013

4.Physiological analysis of the stringent response elicited in an extreme thermophilic bacterium, Thermus thermophilus. Kasai K, Nishizawa T, Takahashi K, Hosaka T, Aoki H, Ochi K. J. Bacteriol. 188, 7111-22, (2006). View articlePMID: 17015650

5.Regulation of the MDM2-p53 pathway by ribosomal protein L11 involves a post-ubiquitination mechanism. Dai MS, Shi D, Jin Y, Sun XX, Zhang Y, Grossman SR, Lu H. J. Biol. Chem. 281, 24304-13, (2006). View articlePMID: 16803902

6.A detailed view of a ribosomal active site: the structure of the L11-RNA complex. Wimberly BT, Guymon R, McCutcheon JP, White SW, Ramakrishnan V. Cell 97, 491-502, (1999). View articlePMID: 10338213

7.Interaction of thiostrepton and elongation factor-G with the ribosomal protein L11-binding domain. Bowen WS, Van Dyke N, Murgola EJ, Lodmell JS, Hill WE. J. Biol. Chem. 280, 2934-43, (2005). View articlePMID: 15492007

8.Essential role of ribosomal protein L11 in mediating growth inhibition-induced p53 activation. Bhat KP, Itahana K, Jin A, Zhang Y. EMBO J. 23, 2402-12, (2004). View articlePMID: 15152193

9.The role of ribosomal protein L11 in class I release factor-mediated translation termination and translational accuracy. Bouakaz L, Bouakaz E, Murgola EJ, Ehrenberg M, Sanyal S. J. Biol. Chem. 281, 4548-56, (2006). View articlePMID: 16371360

10.The roles of ribosomal proteins in the structure assembly, and evolution of the large ribosomal subunit. Klein DJ, Moore PB, Steitz TA. J. Mol. Biol. 340, 141-77, (2004). View articlePMID: 15184028

11.Structure of the base of the L7/L12 stalk of the Haloarcula marismortui large ribosomal subunit: analysis of L11 movements. Kavran JM, Steitz TA. J. Mol. Biol. 371, 1047-59, (2007). View articlePMID: 17599351

12.L11 domain rearrangement upon binding to RNA and thiostrepton studied by NMR spectroscopy. Jonker HR, Ilin S, Grimm SK, Wohnert J, Schwalbe H. Nucleic Acids Res. 35, 441-54, (2007). View articlePMID: 17169991

13.Translational regulation via L11: molecular switches on the ribosome turned on and off by thiostrepton and micrococcin. Harms JM, Wilson DN, Schluenzen F, Connell SR, Stachelhaus T, Zaborowska Z, Spahn CM, Fucini P. Mol. Cell 30, 26-38, (2008). View articlePMID: 18406324

14.Structural properties of ribosomal protein L11 from Escherichia coli. Choli T. Biochem. Int. 19, 1323-38, (1989). PMID: 2483975

15.Multiple-site trimethylation of ribosomal protein L11 by the PrmA methyltransferase. Demirci H, Gregory ST, Dahlberg AE, Jogl G. Structure 16, 1059-66, (2008). View articlePMID: 18611379

16.Recognition of ribosomal protein L11 by the protein trimethyltransferase PrmA. Demirci H, Gregory ST, Dahlberg AE, Jogl G. EMBO J. 26, 567-77, (2007). View articlePMID: 17215866

GO terms

Cross References

Contributing Member Database Entries
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.