Effect of Ultraviolet Irradiation on 30‐S Ribosomal Subunits. Identification of the RNA Region Crosslinked to Protein S7

Ehresmann, Bernard; Backendorf, Claude; Ehresmann, Chantal; Millon, Régine; Ebel, Jean‐Pierre

doi:10.1111/j.1432-1033.1980.tb04423.x

Cited by 42 publications

(13 citation statements)

References 48 publications

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“…studying photocross-linking of protein S7 and 16s RNA in 30s ribosomal subunits found that uracil and methionine were involved in adduct formation. [Other experiments (Ehresmann et al, 1980a) have indicated that cytosine is involved in cross-link formation in the S7-16s RNA system. ]…”

Section: Introductionmentioning

confidence: 97%

“…The photochemical covalent cross-linking of proteins to RNA has been recently exploited as a tool to determine points of contact in RNA-protein complexes. Such systems as ribosomes (Zwieb and Brimacombe, 1979;Ehresmann et al, 1980a;Maly er al., 1980), aminoacyl-tRNA synthetase-tRNA complexes [for reviews, see Ebel et al (1979) and Schimmel (1979)l and RNA viruses (Ehresmann et al, 1980b) have been examined using the photocross-linking technique. To date, two points of contact have been characterized, both in ribosomal systems.…”

Section: Introductionmentioning

confidence: 99%

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Photochemical Addition of Amino Acids and Peptides to Polyuridylic Acid

Shetlar¹,

Carbone

Steady

et al. 1984

Photochem & Photobiology

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The quantum yields for photochemical addition of glycine and the L-amino acids commonly occurring in proteins (excluding proline) to polyuridylic acid have been determined in deoxygenated phosphate buffer at pH 7, using a tluorescamine assay technique. All twenty amino acids were found to be reactive. with cysteine. tryptophan, phenylalanine, tyrosine, arginine, lysine and methionine being the most reactive. The analogous quantum yields for a series of eighteen dipeptides of the form glycyl X (X being one of the commonly occurring amino acids, including proline), of L-alanyl-L-tryptophan, of the tripeptides L-seryl-L-seryl-L-serine and L-threonyl-L-threonyl-L-threonine, of the tetrapeptide 1.-cystine-bis-glycine, and of the lysine derivative N"-acetyllysine were also measured. All were found to be reactive toward photoaddition to poly U.

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Section: Introductionmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

Photochemical Addition of Amino Acids and Peptides to Polyuridylic Acid

Shetlar¹,

Carbone

Steady

et al. 1984

Photochem & Photobiology

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“…Similarly, Ehresmann and his coworkers have presented evidence that S7 can be crosslinked to a site in the region 1261-1266 (A-C-C-U-C-G in Fig. 2A) (16). Therefore, we first compared the nucleotide sequence of this region (1220-1340; see refs.…”

Section: Gene Is Not Inhibited By L1 This and Other Experiments mentioning

confidence: 99%

Feedback regulation of ribosomal protein gene expression in Escherichia coli: structural homology of ribosomal RNA and ribosomal protein MRNA.

Nomura¹,

Yates²,

Dean³

et al. 1980

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

213

106

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Certain ribosomal proteins (r proteins) in Escherichia coli, such as S4 -and S7, function as feedback repressors in the regulation of r-protein synthesis. These proteins inhibit the translation of their own mRNA. The repressor r proteins so far identified are also known to bind specifically to rRNA at an initial stage in ribosome assembly. We have found structural homology between the S7 binding region on 16S rRNA and a region of the mRNA where S7 acts as a translational repressor. Similarly, there is structural homology between one of the reported S4 binding regions on 16S rRNA and the mRNA target site for S4. The observed homology supports the concept that regulation by repressor r proteins is based on competition between rRNA and mRNA for these proteins and that the same structural features of the r proteins are used in their interactions with both rRNA and mRNA.In exponentially growing Escherichia coli cells, the rates of synthesis of most if not all ribosomal proteins (r proteins) are essentially identical to the rate of ribosome accumulation and coordinately regulated in response to environmental changes. A feedback model for translational regulation has been suggested to explain this balanced synthesis of r proteins (1), and there is experimental evidence that supports and refines this model (2-4). In this model, it is proposed that certain free r proteins act as feedback inhibitors of the translation of their own mRNAs and that, as long as the assembly of ribosomes removes r proteins, the corresponding mRNA escapes from the inhibition and continues to direct their synthesis. It has been shown in vitro, by using a protein synthesizing system that has various template DNAs carrying r-protein genes (2) and, in vivo, by examining the effect of overproduction of certain r proteins on the synthesis of other r proteins (3), that L1 (and not Lii) is the translational repressor that regulates the synthesis of both L11 and Li in the LIi operon (see Fig. 1). Similarly, S4 (2, 3), S8 (2), S7 (see below), L4 (4, 5), and L10 (6, 7; unpublished results) have been shown to be translational repressors involved in the regulation of the a, spc, str, S10, and 3 operons, respectively.Repressor r proteins probably interact with a specific region of polycistronic mRNA and cause their inhibitory effects indirectly on distal genes through a "polar effect." For example, the in vitro synthesis of Li from DNA templates that carry the Li gene but lack the promoter and an adjacent segment of the LIi gene is not inhibited by L1. This and other experiments have shown that the site of action of Li is localized in a regionThe publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact. 7084 of the mRNA that includes the beginning part of the Lii message (unpublished data). One plausible way to explain these observations and the balanced synthesis of Lii and Li is to assume that every r...

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“…However, other groups were able to crosslink many other proteins in other types of ribosomes (Paleologue et al, 1985) or with E. coli ribosome and tRNA ribosome complexes, yielding much information of structural interest (Turchinsky et al, 1978). Since the doses used (2-10 x lo5 quantdparticle) are in the same range, the different results reported could be accounted for in part by the different sensitivities of the detection methods: 1251 labeling (Turchinsky et al, 1978), silver staining (Paleologue et al, 1985) and Coomassie blue staining (Moller and Brimacombe, 1975;Ehresmann et al, 1980) and overall in vivo (32P)RNA labeling for detection of crosslinked oligonucleotides.…”

Section: Comparison Of the S4u Induced Crosslinks With Those Obtainedmentioning

confidence: 99%

RNA PROTEIN CROSSLINKS INTRODUCED INTO E. coli RIBOSOMES BY USE OF THE INTRINSIC PROBE 4‐THIOURIDINE

Hajnsdorf

Dubreuil

Bezerra

et al. 1987

Photochem & Photobiology

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Abstract— 70S Ribosome substituted by the uridine photoactivable analogue 4‐thiouridine has been prepared by an in vivo method (substitution level 4.5%). The r‐proteins crosslinked to 16S and 23S rRNA before and after 366‐nm photoactivation were identified. Proteins S2‐S7‐S9/11‐S18 are found linked to 16S RNA in dark‐prepared 30S subunits. Illumination increases uniformly their binding by a factor of 2.5. Similarly, proteins L5‐L15‐L18‐L23‐L28‐L32 are found crosslinked to 23S RNA in dark‐prepared 50S subunits. Photoactivation increases their binding but in addition promotes the covalent linking of proteins L1‐L3‐L4.

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Effect of Ultraviolet Irradiation on 30‐S Ribosomal Subunits. Identification of the RNA Region Crosslinked to Protein S7

Cited by 42 publications

References 48 publications

Photochemical Addition of Amino Acids and Peptides to Polyuridylic Acid

Photochemical Addition of Amino Acids and Peptides to Polyuridylic Acid

Feedback regulation of ribosomal protein gene expression in Escherichia coli: structural homology of ribosomal RNA and ribosomal protein MRNA.

RNA PROTEIN CROSSLINKS INTRODUCED INTO E. coli RIBOSOMES BY USE OF THE INTRINSIC PROBE 4‐THIOURIDINE

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