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Journal ArticleDOI

The assembly of ribosomes.

TLDR
New experimental results that show the highly cooperative nature of the assembly reaction are described; the number of sites, per RNA chain, which can bind ribosomal proteins independently from each other is at most two to three.
Abstract
Functionally active 30S ribosomes can be reconstituted in vitro from 16S RNA and a mixture of 30S ribosomal proteins under certain defined conditions. Our previous studies on the specificity and kinetics of reconstitution are summarized and discussed. The reconstitution reaction is first-order with respect to formation of active 30S ribosomes. The rate-limiting reaction is probably unimolecular, and it represents the structural rearrangement of an intermediate. Presumed reconstitution intermediates, or RI particles, have been isolated from reconstitution mixtures incubated at low temperature. It has been concluded that the reconstitution takes place in stepwise fashion: 16S ribosomes. New experimental results that show the highly cooperative nature of the assembly reaction are described; the number of sites, per RNA chain, which can bind ribosomal proteins independently from each other (i.e., without cooperativity) is at most two to three. Finally, another approach to the study of ribosome assembly in vivo is described. It utilizes cold-sensitive E. coli mutants that are defective in ribosome biosynthesis at low temperature and accumulate incomplete “intermediate” ribosomal particles.

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Citations
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Journal ArticleDOI

Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane

TL;DR: The structure of the SRP and SRP Receptor is described in more detail in detail in the second part of this monograph.
Journal ArticleDOI

Assembly Mapping of 30S Ribosomal Proteins from E. coli

TL;DR: An assembly map of 30S ribosomal subunits has been constructed and it is shown that the assembly reaction is sequential and cooperative.
Journal ArticleDOI

Assembly of Bacterial Ribosomes

TL;DR: The history of the early work on ribosome assembly in Escherichia coli is presented, including a description of in vivo and in vitro intermediates, and the effects of ribosomal proteins in driving these events are explored.
Journal ArticleDOI

Reconstitution of Escherichia coli 30 S ribosomal subunits from purified molecular components.

TL;DR: The results strongly suggest that 21 purified 30 S proteins together with 16 S RNA are sufficient to reconstitute 30 S subunits, and that no essential 30 S components were lost during the fractionation and purification of the30 S proteins.
Journal ArticleDOI

Disassembly and reconstitution of signal recognition particle.

TL;DR: A rapid procedure was developed to disassemble SRP into native protein and RNA components and the proteins are shown to reassociate stoichiometrically with 7SL-RNA to form fully active 11S SRP.
References
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Book ChapterDOI

Assembly and Stability of the Tobacco Mosaic Virus Particle

TL;DR: The structural and physical chemical studies on TMV considered in this chapter provide a picture of the way in which the viral nucleic acid is packaged for transmission, and illustrate some general principles regarding the molecular organization of biological structures.
Journal ArticleDOI

Molecular characterization of ribonucleic acid from Escherichia coli ribosomes

TL;DR: The ribon nucleic acid from purified 30 s, 50 s and 70 s ribosomes of E. coli has been isolated by the phenol and detergent methods and it is suggested that they are heterogeneous; some contain one 23 s ribonucleic acid component, while others contain two 16 s units.
Journal ArticleDOI

Identification and Functional Characterization of the Protein controlled by the Streptomycin-resistant Locus in E. coli

TL;DR: The streptomycin locus of E. coli specifies a 30S ribosomal protein which determines the sensitivity of the 30S subunit to strePTomycin and streptomecin induced errors of translation.
Journal ArticleDOI

Structure and function of E. coli ribosomes. V. Reconstitution of functionally active 30S ribosomal particles from RNA and proteins.

TL;DR: Analysis of the activity of these particles has revealed the functional significance of each of the purified ribosomal split proteins, supporting the hypothesis of spontaneous self assembly.
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