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Aminoacyl-tRNA synthetase mutants degrade protein at a normal rate (1979)

Clark, Jeffrey L. ; Rabe, Julie ; Arfin, Stuart M.

New York, NY [u.a.] : Wiley-Blackwell

Journal of Cellular Physiology 98 (1979), S. 237-239

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Details

ISSN: 0021-9541

Keywords: Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: The stability of both rapidly and slowly degraded proteins in wild type CHO cells is similar to that in three ts aminoacyl-tRNA synthetase mutants at both permissive and non-permissive temperatures, although the degree of tRNA charging in the synthetase mutants differs considerably with temperature. These results indicate that the altered rate of protein breakdown seen under a variety of physiological conditions in eukaryotic systems is not mediated by uncharged tRNA.

Additional Material: 1 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/jcp.1040980125

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