The NH2-terminal domain of Escherichia coli ribosomal protein L11. Its three-dimensional location and its role in the binding of release factors 1 and 2.

Tate, Warren P.; Dognin, Mai J.; Noah, Michael; Stöffler‐Meilicke, Marina; Stöffler, Georg

doi:10.1016/s0021-9258(17)39874-5

Cited by 45 publications

(5 citation statements)

References 39 publications

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“…Other protein synthesis factors may also interact with L11. Either iodination of Y7 within the E. coli L11 N-terminal domain or reaction of antibodies specific for E. coli residues 1-64 interferes with binding of release factor 1 (Tate et al, 1984(Tate et al, , 1986, and stringent factor activity strongly depends on the presence of L11 (Stark et al, 1980). It is possible that the L11 N-terminal domain promotes protein synthesis factor binding to ribosomes by direct interactions and that thiostrepton competes for these interactions; experiments with intact ribosomes will be able to test this speculation.…”

Section: Discussionmentioning

confidence: 99%

“…Ribosomes lacking L11 synthesize protein 2-fold more slowly than normal ribosomes and are correspondingly defective in the elongation factor G (EF-G)-dependent GTPase . L11deficient ribosomes are also defective in release factor 1 (RF1)-dependent termination (Tate et al, 1984) and completely inactive in binding stringent factor, which is responsible for the synthesis of ppGpp and pppGpp in the stringent response (L11 is the relC locus) (Parker et al, 1976;Smith et al, 1980). In addition, L11 forms part of the target site for members of the thiazole family of antibiotics (e.g., thiostrepton).…”

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confidence: 99%

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Cooperative Interactions of RNA and Thiostrepton Antibiotic with Two Domains of Ribosomal Protein L11

1996

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Ribosomal protein L11 interacts with a 58-nucleotide domain of large subunit ribosomal RNA; both the protein and its RNA target have been highly conserved. The antibiotic thiostrepton recognizes the same RNA domain, and binds to the ribosome cooperatively with L11. Experiments presented here show that RNA recognition and thiostrepton cooperativity can be attributed to C- and N-terminal domains of L11, respectively. Under trypsin digestion conditions that degrade Bacillus stearothermophilus L11 to small fragments, the target RNA protects the C-terminal 77 residues from digestion, and thiostrepton and RNA in combination protect the entire protein. A 76-residue C-terminal fragment of L11 was overexpressed and shown to fold into a stable structure binding ribosomal RNA with essentially the same properties as full-length L11. An L11.thiostrepton.RNA complex was 100-200-fold more stable than expected on the basis of L11-RNA and thiostrepton-RNA binding affinities; similar measurements with the C-terminal fragment detected no cooperativity with thiostrepton. L11 function is thus more complex than simple interaction with ribosomal RNA; we suggest that thiostrepton mimics some ribosomal component or factor that normally interacts with the L11 N-terminal domain.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Cooperative Interactions of RNA and Thiostrepton Antibiotic with Two Domains of Ribosomal Protein L11

1996

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“…1C), consistent with the idea that it is dynamic. The different positions of domain 1 in different structures highlight that interactions between domain 1 and the ribosome are dynamic and are likely important at early stages of RF1 binding or during RF1 dissociation, in keeping with functional interaction between RF1 and L11 (27)(28)(29).…”

Section: Mechanism Of Termination On the Uau Sense Codonmentioning

confidence: 99%

Mechanism of premature translation termination on a sense codon

Svidritskiy

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2018

Journal of Biological Chemistry

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Accurate translation termination by release factors (RFs) is critical for the integrity of cellular proteomes. Premature termination on sense codons, for example, results in truncated proteins, whose accumulation could be detrimental to the cell. Nevertheless, some sense codons are prone to triggering premature termination, but the structural basis for this is unclear. To investigate premature termination, we determined a cryo-EM structure of the 70S ribosome bound with RF1 in response to a UAU (Tyr) sense codon. The structure reveals that RF1 recognizes a UAU codon similarly to a UAG stop codon, suggesting that sense codons induce premature termination because they structurally mimic a stop codon. Hydrophobic interaction between the nucleobase of U3 (the third position of the UAU codon) and conserved Ile-196 in RF1 is important for misreading the UAU codon. Analyses of RNA binding in ribonucleoprotein complexes or by amino acids reveal that Ile-U packing is a frequent protein-RNA-binding motif with key functional implications. We discuss parallels with eukaryotic translation termination by the release factor eRF1.

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“…Στο E. coli έχουν απομονωθεί δύο παράγοντες τερματισμού της πρωτεϊνοσύνθεσης: ο RF-1 που αναγνωρίζει τα κωδίκια λήξης UAG και UAA και ο RF-2 που αναγνωρίζει τα κωδίκια λήξης UAA και UGA (Tate et al 1984).…”

Section: η πορεία της μετάφρασης στο Saccharomyces Cerevisiaeunclassified

Μελέτη Της Δομής Και Λειτουργίας Του Ευκαρυωτικού Ριβοσώματος Με Τη Βοήθεια Μεταλλάξεων Επί Γονιδίων Ορισμένων Ριβοσωματικών Πρωτεϊνών Και Ριβοσωματικού RNA Της Ζύμης

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The NH2-terminal domain of Escherichia coli ribosomal protein L11. Its three-dimensional location and its role in the binding of release factors 1 and 2.

Cited by 45 publications

References 39 publications

Cooperative Interactions of RNA and Thiostrepton Antibiotic with Two Domains of Ribosomal Protein L11

Cooperative Interactions of RNA and Thiostrepton Antibiotic with Two Domains of Ribosomal Protein L11

Mechanism of premature translation termination on a sense codon

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