Identification of the Proteins Associated with Subparticles Produced by Mild Ribonuclease Digestion of 30S Ribosomal Particles from
            <i>Escherichia coli</i>

Schendel, Peter L.; Maeba, P.; Craven, Gary R.

doi:10.1073/pnas.69.3.544

Cited by 16 publications

(2 citation statements)

References 21 publications

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“…This is obviously an important consideration, when EDTA particles are used for studies on the organization of the ribosomal components. In particular, several authors have reported the isolation of specific ribo-nucleoprotein fragments from EDTA-treated [3-51 or de-salted [6] particles, which would suggest that the proteins remain specifically located on the RNA. However, in our own studies on specific fragments from E. coli ribosomes, we have been unable to obtain fragments from either the 30s or SOS sub-particles in the presence of EDTA which satisfy our rigorous criteria for specificity [7,8].…”

Section: Introductionmentioning

confidence: 99%

Random exchange of ribosomal proteins in EDTA sub‐particles

1975

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Section: Introductionmentioning

confidence: 99%

Random exchange of ribosomal proteins in EDTA sub‐particles

1975

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“…The binding sites of proteins S4 and S16 are localized in the 5' domain, and those of S7, S9, S13 and S19, in the 3' major domain (4,5 (30). Several groups have studied ribonucleoprotein fragments derived from intact (as distinct from partially reconstituted) 30 S ribosomes and have identified their proteins and in some cases also their RNA components (16,(31)(32)(33)(34)(35)(36).…”

Section: Discussionmentioning

confidence: 99%

A ribonucleoprotein fragment of the 30 S ribosome of E. coli: evidence for long range RNA-RNA interactions

et al. 1982

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A stable homogeneous ribonucleoprotein fragment of the 30 S ribosomal subunit of E. coli has been prepared by mild nuclease digestion and heating in a constant ionic environment. The fragment contains about half of the 16 S ribosomal RNA and six proteins: S4, S7, S9, S13, S16 and S19. The RNA moiety contains the reported binding sites of all six proteins. After deproteinization, 80% of the RNA migrated as two major electrophoretic bands, which were isolated and sequenced. Each band contained sequences from the 5' and 3' thirds of the 16 S RNA but none from the central third. That these two noncontiguous RNA domains migrated together electrophoretically in Mg++-containing gels after deproteinization constitutes direct evidence that the 16 S RNA is folded in the intact ribosome so as to bring the two domains close together and that there are RNA-RNA interactions between them in the presence of Mg++.

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The assembly of the 30s ribosomal subunit of Escherichia coli

Kurland¹

1974

J Supramol Struct

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The present article is concerned with ribosome assembly. However, this theme is really only a device which is introduced t o explore the functions of that two-thirds of the prokaryotic ribosome which is RNA. A close look at ribosome assembly turns out to be a convenient way t o approach this problem.A clear distinction between ribosome assembly in vivo and the reconstitution process in vitro must be made at the outset in order t o avoid errors in the interpretation of the different sets o f data. The data utilized here concern the components of the 30s subunit of the Escherichia coli ribosome and their behavior in the reconstitution system of Traub and Nomura (1). A strong hint that this system may turn out be a subtle but extremely useful artifact is the simple fact that under the same conditions in vitro the reproducible reconstitution of active E. coli 50s subunits has so far eluded a number of expert laboratories.Potential sources of artifacts in the in vitro system are easy t o point out. First, the processing of precursor RNA in the course of assembly in vivo involves the cleavage as well as the methylation of specific FWA sequences (2, 3 ) . Quite possibly a parallel processing of proteins may be operative in vivo (4). Accordingly, the reconstitution from mature RNA and protein in vitro may be distinguished from assembly in vivo by differences in the structures of the ribosomal components involved in these two processes. Second, we must consider the possibility that there are factors functioning in vivo which can increase the rate of assembly but which are absent from the purified ribosomes (5).The paradigm for such factors is seen in a much simpler system ~ namely, the renaturation of reduced ribonuclease. Here, an enzyme has been described which lowers by orders of magnitude the time required t o renature reduced nuclease. It does so merely by catalyzing the random exchange rate of disulfide bonds (6). Given the extraordinary complexity of the ribosome it is quite possible that analogous factors are required t o accelerate assembly in vivo. For these reasons we might expect the reconstitution process in vitro t o proceed via kinetic pathways which are quite different from those preferred in vivo. 1780 1974 Alan R.

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Identification of the Proteins Associated with Subparticles Produced by Mild Ribonuclease Digestion of 30S Ribosomal Particles from Escherichia coli

Cited by 16 publications

References 21 publications

Random exchange of ribosomal proteins in EDTA sub‐particles

Random exchange of ribosomal proteins in EDTA sub‐particles

A ribonucleoprotein fragment of the 30 S ribosome of E. coli: evidence for long range RNA-RNA interactions

The assembly of the 30s ribosomal subunit of Escherichia coli

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