Ribosomal proteins L4 and L22 both have a globular domain that sits on the surface of the large ribosomal subunit and an extended loop that penetrates its core. The tips of both loops contribute to the lining of the peptide exit tunnel and have been implicated in a gating mechanism that might regulate the exit of nascent peptides. Also, the extensions of L4 and L22 contact multiple domains of 2...

We characterized the effects of classical erythromycin resistance mutations in ribosomal proteins L4 and L22 of the large ribosomal subunit on the kinetics of erythromycin binding. Our data are consistent with a mechanism in which the macrolide erythromycin enters and exits the ribosome through the nascent peptide exit tunnel, and suggest that these mutations both impair passive transport throu...

1 2 3 4 5 6 7 8 1 e0 e9 e11 e12 e10 e7 e15 2 e4 e2 e5 e6 L L L e13 3 e1 e3 e8 L L L L e16 4 L L L L L L e17 5 e0 e11 e12 e10 e9 L e15 6 e4 e2 e6 L19 e7 e5 L20 e13 7 e1 e3 L24 e8 L23 L22 e16 8 L25 L26 L30 L27 L28 L29 e17 9 e0 e12 e10 L31 e11 e9 e15 10 e4 e2 L19 L20 e6 e7 e13 11 e1 e3 L22 L23 L24 e8 e16 12 L L25 L26 L29 L30 L27 L28 e17 13 e0 e10 L21 e12 e9 e11 e15 14 e4 e2 e7 e6 L20 L19 e13 15 e1...

Resistance to macrolides and ketolides occurs mainly via alterations in RNA moieties of the drug-binding site. Using an A2058G mutant of Mycobacterium smegmatis, additional telithromycin resistance was acquired via deletion of 15 residues from protein L22. Molecular modeling, based on the crystal structure of the large ribosomal subunit from Deinococcus radiodurans complexed with telithromycin,...

Mutations in the ribosomal protein L22 that impair peptide-mediated translation arrest in Escherichia coli have been shown to reduce the expression of several genes, including secA, which encodes an ATPase that drives protein export via the Sec pathway. Here, we used a comparative proteomic approach to obtain insight into the global effects of the L22(Δ82-84) mutation on gene expression and pro...

Article history: Received 3 March 2010 Available online 3 November 2010 JEL classification: L22 L51 O31 O38