Ribosomal proteins contacting with deacylated tRNA in the S‐site of the translating ribosome

Abdurashidova, G.G.; Turchinsky, M.F.; Budowsky, E.I.

doi:10.1016/0014-5793(81)80755-7

Cited by 20 publications

(7 citation statements)

References 17 publications

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“…It has been shown earlier that these irradiation conditions (15 -20 quanta/nucleotide) do not cause significant conformational changes of 30-S subparticles [28] or of complexes of 7 0 4 ribosomes with poly(U) and Phe-tRNAPhe [30]. This fact suggests that these doses fixed only native RNA-protein contacts within the 30-S subparticles.…”

Section: Resultsmentioning

confidence: 83%

“…We have tried it earlier in order to identify ribosomal proteins interacting with 1 6 3 RNA [28,29] and proteins contacting tRNA at the A, P and S sites within 7 0 3 ribosomes [30,32]. This technique has also been used for detecting 30-S ribosomal proteins interacted with poly(U) [32] and poly(s4U) [33].…”

Section: -S Subunits Of E Coli Ribosomes Form Complexes Withmentioning

confidence: 99%

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Proteins of the 30‐S Subunit of Escherichia coli Ribosomes which Interact Directly with Natural mRNA

Broude

Kussova

Mecvedeva

et al. 1983

European Journal of Biochemistry

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Ultraviolet irradiation (254 nm) of the complexes of MS2 phage RNA (mRNA) and the 30-S subunits of E.sclzeviclzia coli ribosomes prepared at 0 'C and 37 'C in the presence and absence of initiation factor 3 (IF-3) causes cross-linking of mRNA with proteins S3, S4, S5, S7, S9, S18 and IF-3. Hence, these proteins interact directly with mRNA within the complex 30-S-subunit . mRNA.Addition of IF-3 results in an increase of the rate of complex formation and decrease of its dissociation rate. The addition of IF-3 changes the relative amounts of cross-linked proteins (mainly S3, S4 and S18).Decreasing the temperature from 37 'C to 0 "C not only decelerates the complex formation rate but also changes the relative amount of cross-linked proteins, indicating the influence of the conditions on the structure of the complex.It is well known that prokaryotic messenger RNAs are polycistronic and initiation can take place at the internal sites of the RNA [I]. The selection of initiation sites in messenger RNA depends on RNA conformation ; therefore unfolding of RNA allows the ribosome to interact with additional AUG codons [2,3]. On the other hand, the specificity of initiation is determined by the ribosome itself. For instance, ribosomes of Bacillus stearothermophilus translate predominantly the A protein on RNAs of phages R17 and f 2 [2,4] , whereasEscherichia coli ribosomes translate the coat protein on the same messengers [2].Up to now, the only known molecular interactions involved in initiation complex formation are Shine-Dalgarno interactions, i.e. the complementary binding of the nucleotide sequence near the 3' end of 16-S rRNA and the region in messenger RNA 5'-distal to the initiation codon [S]. However, it has been shown that E. coli ribosomes are able to translate messenger RNAs which do not contain the ShineDalgarno sequence [6]. At the same time eukaryotic ribosomes which possess no polypyrimidine sequence near the 3' end of 1 6 3 RNA [7] also translate RNA from phages giving rise to the same proteins as E. coli ribosomes [8-101. That implies that the initiation complex stabilisation leading to specific interaction between ribosones and messenger RNA depends on a multiplicity of interactions between the respective sites of mRNA and ribosomal components, the relative role of which can change depending on the ribosome and cistron structure. Therefore the structural study of messenger RNA and ribosomal components involved in initiation complex formation is a prerequisite for understanding the principles of initiation. ~~Abhreviarions. Poly(U), poly(uridy1ic acid); poly(s4U), poly(4-thiouridylic acid); IF-3, initiation factor 3 ; rRNA, ribosomal R N A ; 3 0 s . MS2 RNA, complex between 3 0 3 subunits and MS2 RNA; 3 0 3 IF3 . MS2 RNA, complex containing 30-S subunits, IF-3 and MS2 RNA.En;-vmrs. RNase A (EC 3.1.27.5); RNase TI (EC 3.1.27.3); alkaline phosphatase (EC 3.1.3.1); polynucleotide kinase (EC 2.7.1.78). 30-S subunits of E. coli ribosomes form complexes withRNAs from phages in the absence of initiator tRNA [I 1 ...

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Section: Resultsmentioning

confidence: 83%

Section: -S Subunits Of E Coli Ribosomes Form Complexes Withmentioning

confidence: 99%

Proteins of the 30‐S Subunit of Escherichia coli Ribosomes which Interact Directly with Natural mRNA

Broude

Kussova

Mecvedeva

et al. 1983

European Journal of Biochemistry

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“…We suggest proteins L3, L6, L23 and L25 as being cross-linked to 23 S rRNA directly in the initiation complex. On the other hand, protein $5 was found previously to crosslink to fMet-tRNA~ et or AcPhe-tRNA vhe in the 30 S initiation complex or its analog [11,12]. This protein was also labeled with photoactivated tRNA~ ~t derivatives in the 70 S initiation complex [9].…”

Section: Resultsmentioning

confidence: 98%

Differences in 23 S rRNA‐protein neighbourhood in Escherichia coli 70 S ribosomes and 70 S initiation complex

et al. 1989

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rRNA-protein cross-links in free E. coil 35S-labeled 70 S ribosomes and in the initiation complex 3sS-labeled 70 S ribosome-AUGUr • fMet-tRNAff et were studied with the aid of a new type of binuclear Pt(II) compound -dichlorotetraammine(1,6-hexamethylenediaminediplatinum) dichloride. The use of this reagent allowed us to reveal differences in the rRNA-protein neighbourhood in free 70 S ribosomes and in the initiation complex. Proteins L3, L6, L23 and L25 were shown to cross-link to 23 S rRNA only in the initiation complex, whereas proteins L1, L13, L14, L16, L17, L18, L22, L28 and S1 did so in both free ribosomes and the complex. 16 S rRNA was found to be cross-linked preferentially to a single protein, S 1, in both states of the ribosomes.

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“…The molar ratio of NAcPhe-tRNA pne to 30 S subunit in the complex formed was 0.9. After addition of 50 S subunits to this complex more than 90°7o of NAcPhe was transferred to puromycin (see [13]). …”

Section: Resultsmentioning

confidence: 99%

“…Each of the bands 1-3 contains a single protein, which was identified according to [13] as $7, $5 and $9, respectively. Therefore, each of these bands contains the product of tRNA cross-linking to a particular protein molecule, while the products of tRNA cross-linking with two or more pro- Fig.3.…”

Section: Resultsmentioning

confidence: 99%

Nucleotide residues of tRNA, directly interacting with proteins within the complex of the 30 S subunit of E. coli ribosome with poly(U) and NAcPhe‐tRNA^Phe

1989

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With the aid of photoinduced tRNA-protein cross-linking, nucleotide residues A21, U45 and U60 were shown to interact directly with proteins $5, $7 and $9 respectively, in the complex of the 30 S subunit of E. coli ribosome with poly(U) and NAcPhe-tRNA TM. These nucleotide residues are located in the central part of the L-form in the tertiary structure of RNA.Ribosomal subunit; 30 S' poly(U) • NAcPhe-tRNA vhe complex; Ultraviolet-induced crosslinking; tRNA-protein interaction

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Ribosomal proteins contacting with deacylated tRNA in the S‐site of the translating ribosome

Cited by 20 publications

References 17 publications

Proteins of the 30‐S Subunit of Escherichia coli Ribosomes which Interact Directly with Natural mRNA

Proteins of the 30‐S Subunit of Escherichia coli Ribosomes which Interact Directly with Natural mRNA

Differences in 23 S rRNA‐protein neighbourhood in Escherichia coli 70 S ribosomes and 70 S initiation complex

Nucleotide residues of tRNA, directly interacting with proteins within the complex of the 30 S subunit of E. coli ribosome with poly(U) and NAcPhe‐tRNA^Phe

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Ribosomal proteins contacting with deacylated tRNA in the S‐site of the translating ribosome

Cited by 20 publications

References 17 publications

Proteins of the 30‐S Subunit of Escherichia coli Ribosomes which Interact Directly with Natural mRNA

Proteins of the 30‐S Subunit of Escherichia coli Ribosomes which Interact Directly with Natural mRNA

Differences in 23 S rRNA‐protein neighbourhood in Escherichia coli 70 S ribosomes and 70 S initiation complex

Nucleotide residues of tRNA, directly interacting with proteins within the complex of the 30 S subunit of E. coli ribosome with poly(U) and NAcPhe‐tRNAPhe

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Nucleotide residues of tRNA, directly interacting with proteins within the complex of the 30 S subunit of E. coli ribosome with poly(U) and NAcPhe‐tRNA^Phe