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Supramolecular organization of the mammalian translation system / B.S. Negrutskii, R. Stapulionis, M.P. Deutscher
Type of publication
Straipsnis Web of Science duomenų bazėje / Article in Web of Science database (S1a)
Author(s)
Negrutskii, Boris Sergejevic | University of Connecticut Health Center |
Department of Biochemistry, University of Connecticut Health Center | |
Deutscher, Muray P | University of Connecticut Health Center |
Title
Supramolecular organization of the mammalian translation system / B.S. Negrutskii, R. Stapulionis, M.P. Deutscher
Publisher (trusted)
National Academy of Sciences |
Is Referenced by
Date Issued
Date Issued |
---|
1994-02-01 |
Extent
p. 964-968.
Is part of
Proceedings of the National Academy of Sciences of the United States of America. Washington : National Academy of Sciences, 1994, vol. 91, no. 3.
Version
Originalus / Original
Field of Science
Abstract
Although evidence suggests that the protein synthetic machinery is organized within cells, this point has been difficult to prove because any organization that might exist is lost upon preparation of the cell-free systems usually used to study translation in vitro. To examine this process under conditions more representative of the intact cell, we have developed an active protein-synthesizing system using Chinese hamster ovary (CHO) cells permeabilized with the plant glycoside saponin. This procedure renders cells permeable to trypan blue and exogenous tRNA, but there is little release of endogenous macromolecules. Protein synthesis in this system proceeds at the same rate as that in intact cells and is about 40-fold faster than that in a cell-free system prepared from the same cells. Active protein synthesis in this system requires the addition of only Mg2+, K+, and creatine phosphate, with a small further stimulation by ATP and an amino acid mixture; no exogenous macromolecules are necessary. The proteins synthesized in this system are indistinguishable from those made by the intact cell, and the channeling of aminoacyl-tRNA observed in vivo is maintained. Our data suggest that the permeabilized cell system retains the protein-synthesizing capabilities of the intact cell and presumably its internal structure as well. Studies with this system demonstrate that the protein-synthesizing apparatus is highly organized and that its macromolecular components are not freely diffusible in mammalian cells.
Type of document
type::text::journal::journal article
ISSN (of the container)
0027-8424
WOS
A1994MV27800030
Other Identifier(s)
(LSMU ALMA)990000384730107106
Coverage Spatial
Jungtinės Amerikos Valstijos / United States of America (US)
Language
Anglų / English (en)
Bibliographic Details
26