Structural arrangement of tRNA binding sites on Escherichia coli ribosomes, as revealed from data on affinity labelling with photoactivatable tRNA derivatives

Graifer, D. M.; Babkina, G.T.; Matasova, Natalya B; Vladimirov, Sergei N; Карпова, Г. Г.; Vlassov, V. V.

doi:10.1016/0167-4781(80)90002-0

Cited by 28 publications

(15 citation statements)

References 27 publications

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“…2). The latter protein, which can be cross-linked to P-site tRNAs (34), is also located near the PTC (20). We showed that loss of EF-P, which assists the incorporation of Pro residues into nascent peptides, also led to increased expression of mgtA at high Mg 2+ (Fig.…”

Section: Unique Mutations That Clarify the Role Of Mgtl Translation Imentioning

confidence: 76%

Mg ²⁺ regulates transcription of mgtA in Salmonella Typhimurium via translation of proline codons during synthesis of the MgtL peptide

Gall

Datsenko

Figueroa‐Bossi

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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In Salmonella enterica serovar Typhimurium, Mg 2+ limitation induces transcription of the mgtA Mg 2+ transport gene, but the mechanism involved is unclear. The 5′ leader of the mgtA mRNA contains a 17-codon, proline-rich ORF, mgtL, whose translation regulates the transcription of mgtA [Park S-Y et al. (2010) Cell 142:737-748]. Rapid translation of mgtL promotes formation of a secondary structure in the mgtA mRNA that permits termination of transcription by the Rho protein upstream of mgtA, whereas slow or incomplete translation of mgtL generates a different structure that blocks termination. We identified the following mutations that conferred high-level transcription of mgtA at high [Mg 2+ ]: (i) a base-pair change that introduced an additional proline codon into mgtL, generating three consecutive proline codons; (ii) lesions in rpmA and rpmE, which encode ribosomal proteins L27 and L31, respectively; (iii) deletion of efp, which encodes elongation factor EF-P that assists the translation of proline codons; and (iv) a heat-sensitive mutation in trmD, whose product catalyzes the m 1 G37 methylation of tRNA Pro . Furthermore, substitution of three of the four proline codons in mgtL rendered mgtA uninducible. We hypothesize that the proline codons present an impediment to the translation of mgtL, which can be alleviated by high [Mg 2+ ] exerted on component(s) of the translation machinery, such as EF-P, TrmD, or a ribosomal factor. Inadequate [Mg 2+ ] precludes this alleviation, making mgtL translation inefficient and thereby permitting mgtA transcription. These findings are a significant step toward defining the target of Mg 2+ in the regulation of mgtA transcription.MgtA Mg 2+ transporter | MgtL leader peptide | 50S ribosomal proteins | EF-P translation factor | TrmD methyltransferase

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Section: Unique Mutations That Clarify the Role Of Mgtl Translation Imentioning

confidence: 76%

Mg ²⁺ regulates transcription of mgtA in Salmonella Typhimurium via translation of proline codons during synthesis of the MgtL peptide

Gall

Datsenko

Figueroa‐Bossi

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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“…A direct interaction is suggested by A site tRNA cross-links to L9 that place it within 13Å of the decoding center during the decoding step (42). How this data is to be reconciled with evidence that places L9 just below the lateral protuberance is uncertain, but the length of the protein (82Å) is nearly one third the width of the large subunit.…”

Section: Ribosomal Protein L9 and Take-offmentioning

confidence: 95%

Coupling of Open Reading Frames by Translational Bypassing

Herr

Atkins

Gesteland

2000

Annu. Rev. Biochem.

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Translational bypassing joins the information found within two disparate open reading frames into a single polypeptide chain. The underlying mechanism centers on the decoding properties of peptidyl-transfer RNA (tRNA) and involves three stages: take-off, scanning, and landing. In take-off, the peptidyl-tRNA/messenger RNA (mRNA) complex in the P site of the ribosome dissociates, and the mRNA begins to move through the ribosome. In scanning, the peptidyl-tRNA probes the mRNA sliding through the decoding center. In landing, the peptidyl-tRNA re-pairs with a codon with which it can form a stable interaction. Although few examples of genes are known that rely on translational bypassing to couple open reading frames, ribosomes appear to have an innate capacity for bypassing. This suggests that the strategy of translational bypassing may be more common than presently appreciated. The best characterized example of this phenomenon is T4 gene 60, in which a complex set of signals stimulates bypassing of 50 nucleotides between the two open reading frames. In this review, we focus on the bypassing mechanism of gene 60 in terms of take-off, scanning, and landing.

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“…This crosslink is inconsistent with data that suggest L9 binds in domain V of the 23 S rRNA and probably only reflects proximity of helix 58 to L9 . Affinity labeling of L9 by aminoacyl site (A-site) tRNA also places L9 near (within 13 Å ) the peptidyl transferase center (Graifer et al, 1989). Although L9 is not required for peptidyl transferase activity (Hampl et al, 1981), the effect of mutants on bypass provides a system for probing the role of L9 in translation.…”

Section: Introductionmentioning

confidence: 97%

Ribosomal Protein L9 Interactions with 23 S rRNA: The Use of a Translational Bypass Assay to Study the Effect of Amino Acid Substitutions

Adamski

Atkins

Gesteland

1996

Journal of Molecular Biology

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Structural arrangement of tRNA binding sites on Escherichia coli ribosomes, as revealed from data on affinity labelling with photoactivatable tRNA derivatives

Cited by 28 publications

References 27 publications

Mg ²⁺ regulates transcription of mgtA in Salmonella Typhimurium via translation of proline codons during synthesis of the MgtL peptide

Mg ²⁺ regulates transcription of mgtA in Salmonella Typhimurium via translation of proline codons during synthesis of the MgtL peptide

Coupling of Open Reading Frames by Translational Bypassing

Ribosomal Protein L9 Interactions with 23 S rRNA: The Use of a Translational Bypass Assay to Study the Effect of Amino Acid Substitutions

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Structural arrangement of tRNA binding sites on Escherichia coli ribosomes, as revealed from data on affinity labelling with photoactivatable tRNA derivatives

Cited by 28 publications

References 27 publications

Mg 2+ regulates transcription of mgtA in Salmonella Typhimurium via translation of proline codons during synthesis of the MgtL peptide

Mg 2+ regulates transcription of mgtA in Salmonella Typhimurium via translation of proline codons during synthesis of the MgtL peptide

Coupling of Open Reading Frames by Translational Bypassing

Ribosomal Protein L9 Interactions with 23 S rRNA: The Use of a Translational Bypass Assay to Study the Effect of Amino Acid Substitutions

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Mg ²⁺ regulates transcription of mgtA in Salmonella Typhimurium via translation of proline codons during synthesis of the MgtL peptide

Mg ²⁺ regulates transcription of mgtA in Salmonella Typhimurium via translation of proline codons during synthesis of the MgtL peptide