The Cation Specificity for the Maintenance of the Structure and Function of the 30S Ribosomal Subunit of Escherichia Coli PDF Download
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Author: Richard Louis Weiss
Publisher:
ISBN:
Category : Cations
Languages : en
Pages : 264
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Author: Richard Louis Weiss
Publisher:
ISBN:
Category : Cations
Languages : en
Pages : 264
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Author: Brian William Kimes
Publisher:
ISBN:
Category : Cations
Languages : en
Pages : 348
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Author: Paul Voynow
Publisher:
ISBN:
Category : Escherichia coli
Languages : en
Pages : 190
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Author: American Chemical Society. Committee on Professional Training
Publisher:
ISBN:
Category : Biochemistry
Languages : en
Pages : 920
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Faculties, publications and doctoral theses in departments or divisions of chemistry, chemical engineering, biochemistry and pharmaceutical and/or medicinal chemistry at universities in the United States and Canada.
Author: Melissa Allene Buck
Publisher:
ISBN:
Category :
Languages : en
Pages : 434
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Author: Jennifer Anne Maki
Publisher:
ISBN:
Category :
Languages : en
Pages : 206
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The prokaryotic ribosome is a 2.5 MDa particle comprised of two asymmetric subunits, the large (50S) and small (30S) subunits. The large subunit contains two RNAs (5S and 23S) in addition to thirty-four proteins. The small subunit consists of one RNA (16S rRNA) and twenty-one proteins. Although the crystal structure has been solved, much remains to be revealed concerning the assembly of this macromolecular structure. Our laboratory is focused on the assembly of the small subunit. In vitro assembly of this structure was achieved in the late 1960's and early 1970's. At low temperature when 16S rRNA and all of the small subunit proteins are incubated together, only a subset of the proteins are able to associate with the RNA and a particle termed Reconstitution Intermediate (RI, 2IS) results. When RI particles are heat treated, a conformational rearrangement occurs and RI* (26S) particles result that are capable of complete assembly with the remainder of the small subunit proteins, even at low temperature, to form functional 30S subunits. In vitro 30S subunit assembly requires long incubation periods, high ionic strength, and heat treatment. In light of these strict requirements, we hypothesized that assembly factors must exist in vivo to facilitate this crucial assembly process, making it accurate and efficient. We have identified the DnaK chaperone system as one such factor. The purified DnaK chaperone system is sufficient to facilitate in vitro 30S subunit assembly at low temperature, forming 30S particles that co-sediment, have the same protein complement, bind tRNA, and participate in polyphenylalanine synthesis like 30S subunits. Additionally, the association behavior of the DnaK chaperone system components with pre-30S particles in vitro was observed and found to be very similar to their association with substrate in their well-characterized protein folding role. Lastly, it was determined that DnaK binds small subunit components in vivo, including pre-processed 16S rRNA. This is the first evidence clearly demonstrating a direct link between the DnaK chaperone system and the assembly of ribosomes in E. coli, and the first instance in which an extra-ribosomal assembly factor has been shown to facilitate 30S subunit assembly in vitro.
Author: Xerox University Microfilms
Publisher:
ISBN:
Category : Dissertations, Academic
Languages : en
Pages : 960
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Author:
Publisher:
ISBN:
Category : Union catalogs
Languages : en
Pages : 536
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Includes entries for maps and atlases.
Author: Federation of American Societies for Experimental Biology
Publisher:
ISBN:
Category : Biology
Languages : en
Pages : 1918
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Author:
Publisher:
ISBN:
Category : Medicine
Languages : en
Pages : 1320
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