Nucleotide Sequences of <i>Escherichia coli</i> 16‐S RNA Associated with Ribosomal Proteins S7, S9, S10, S14 and S19

Yûki, Atsushi; Brimacombe, Richard

doi:10.1111/j.1432-1033.1975.tb02203.x

Cited by 70 publications

(74 citation statements)

References 25 publications

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“…As before (3) two second dimension gels were made for each first dimension gel strip, the upper half of the latter being run on a 10% second dimension gel, and the lower half on a 20% gel. After electrophoresis, the cross-linked complexes were located on the gels by autoradiography, and were extracted in the usual manner (17). In one case (complex E, see results), the isolated complex was further-digested with ribonuclease T1 in the presence of 50 4g of unlabelled carrier tRNA, followed by separation on a second two-dimensional gel, exactly as described pre (18), and in some cases tertiary digestions were made, as described (4).…”

Section: Methodsmentioning

confidence: 99%

Investigation of the tertiary folding ofEscherichia coli16s RNA byin situintra-RNA crosslinking within 30S ribosomal subunits

Atmadja

Brimacombe

Blöcker³

et al. 1985

Nucl Acids Res

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Intra-RNA cross-links were introduced into E. coli 30S ribosomal subunits by mild ultraviolet irradiation. The subunits were partially digested with cobra venom nuclease, followed in some cases by a second partial digestion with ribonuclease H in the presence of the hexanucleotide d-(CTTCCC). The cross-linked RNA complexes were separated by two-dimensional gel electrophoresis and the sites of cross-linking analysed by our published procedures. Tertiary structural cross-links in the 16S RNA were identified between positions 31 and 48, between oligonucleotides 1090-1094 and 1161-1164, and between oligonucleotides 1125-1127 and 1280-1281. The first of these imposes a rigid constraint on the relative orientations of helices 3 and 4 of the 16S secondary structure. A further tertiary cross-link (which could not be precisely localised) was found between regions 1-72 and 1020-1095, and secondary structural cross-links were identified between positions 497 and 545-548, and positions 1238-1240 and 1298.

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Section: Methodsmentioning

confidence: 99%

Investigation of the tertiary folding ofEscherichia coli16s RNA byin situintra-RNA crosslinking within 30S ribosomal subunits

Atmadja

Brimacombe

Blöcker³

et al. 1985

Nucl Acids Res

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“…[6][7]), and several of these fragments have been found to contain S7. Further, it has recently been shown that S7 is the only 30-S protein which can be specifically cross-linked to any large extent to RNA by irradiation with ultraviolet light [8].…”

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Studies on the Environment of Protein S7 within the 30‐S Subunit of Escherichia coli Ribosomes

Rinks

Yûki

Brimacombe

1976

European Journal of Biochemistry

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Analyses are described of three types of ribosomal fragment, all derived from the well-characterized ribonucleoprotein species consisting of proteins S7, S9, S 10, S 14 and S 19, together with RNA from sections 0'-D-E'-K-P-P'-E-A of the 16-S sequence.1. When 30-S subunits were hydrolysed with ribonuclease T, in the presence of deoxycholate in addition to the components previously described, a fragment could be isolated which contained only proteins S7 and S19, together with minor amounts of S13 or S14. Oligonucleotide analysis of this fragment showed that it contained RNA from sections 0'-E' and P-A of the 16-S RNA, but that section K (from the middle of this area) was missing.2. It has previously been shown that when 30-S subunits are irradiated with ultraviolet light, protein S7 is the primary target of cross-linking of protein to RNA. By making use of this reaction, ribonucleoprotein fragments were isolated from irradiated 30-S subunits, the unbound proteins were removed, and RNA fragments containing covalently linked protein S7 were identified. It was possible to demonstrate that the site of cross-linking lies within the 0'-A region of the 26-S RNA, and more precise experiments showed that this site almost certainly is in the P-A region.3. When the parent five-protein ribonucleoprotein fragment (above) was deproteinized under very mild conditions, RNA complexes could be isolated which consisted of non-contiguous sequences, but which migrated as a single species into a polyacrylamide gel. Analysis of one of these complexes showed that it contained sequences from sections 0'-E' and P-A, but that section K was missing (cf: first paragraph above). This demonstrated that these two separate regions of RNA interact within the 30-S subunit, independently of the presence of protein.

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“…P. Ebel for helpful discussions throughout the course of' this work, and to Miss M. Delfau for her technical assistance. The work was financially supported by the Centre Nurional dr 10 Recherche Scirntifique and by the Delegation GPntWe a la Ri,chcrc,hc …”

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RNA Sequences Associated with Proteins L1, L9, and L5, L18, L25, in Ribonucleoprotein Fragments Isolated from the 50‐S Subunit of Escherichia coli Ribosomes

Branlant

Krol

Sri-Widada

et al. 1976

European Journal of Biochemistry

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32P-labelled 50-S subunits froin Escherichiu coli ribosomes were hydrolysed under conditions known to give rise to two specific ribonucleoprotein fragments, containing proteins L 1, L9, and L5, L 18 and L 25 respectively. RNA corresponding to these ribonucleoproteins was isolated and purified, and the various RNA fragments obtained were subjected to oligonucleotide analysis.The results showed that the RNA associated with proteins L 1 and L 9 was very similar to the RNA found with protein L 1 after controlled digestion of 23-S-RNA . L 1 complexes (described elsewhere) ; this RNA lies within a region 550 -1000 nucleotides from the 3' terminus of 23-S RNA. The RNA associated with proteins L5, L18, and L25 consisted predominantly of two species of similar size. One was 5-S RNA, and the other a fragment of 23-S RNA, lying within the region 450-1000 nucleotides from the 3' terminus.

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Nucleotide Sequences of Escherichia coli 16‐S RNA Associated with Ribosomal Proteins S7, S9, S10, S14 and S19

Cited by 70 publications

References 25 publications

Investigation of the tertiary folding ofEscherichia coli16s RNA byin situintra-RNA crosslinking within 30S ribosomal subunits

Investigation of the tertiary folding ofEscherichia coli16s RNA byin situintra-RNA crosslinking within 30S ribosomal subunits

Studies on the Environment of Protein S7 within the 30‐S Subunit of Escherichia coli Ribosomes

RNA Sequences Associated with Proteins L1, L9, and L5, L18, L25, in Ribonucleoprotein Fragments Isolated from the 50‐S Subunit of Escherichia coli Ribosomes

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