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 … expand

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 [ PUBMED:12954336 PUBMED:17095013 PUBMED:18406324 PUBMED:17015650 PUBMED:16803902 PUBMED:17169991 PUBMED:16371360 PUBMED:15492007 PUBMED:15184028 PUBMED:15152193 PUBMED:17599351 PUBMED:10338213 ].

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 [ PUBMED:2167467 ], 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 [ PUBMED:18406324 PUBMED:10338213 PUBMED:17215866 PUBMED:18611379 ]. In E. coli, the C-terminal half of uL11 has been shown [ PUBMED:2483975 ] to be in an extended and loosely folded conformation and is likely to be buried within the ribosomal structure.