von Ehrenstein, Günter and Weisblum, Bernard and Benzer, Seymour (1963) The Function of sRNA as Amino Acid Adaptor in the Synthesis of Hemoglobin. Proceedings of the National Academy of Sciences of the United States of America, 49 (5). pp. 669-675. ISSN 0027-8424 http://resolver.caltech.edu/CaltechAUTHORS:EHRpnas63
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According to the adaptor hypothesis of Crick  and Hoagland , the position of a particular amino acid in a polypeptide chain is determined, not by direct interaction between amino acid and template, but through the mediation of an sRNA molecule that functions as an adaptor. The hypothesis was tested by Chapeville et al.  in a cell-free protein-synthesizing system from E. coli, using a synthetic polynucleotide as template. Cysteine attached to sRNA was converted to alanine, forming an Ala-sRNACYSH hybrid (Fig. 1). The alanine was transferable into polypeptide in response to poly UG, which ordinarily stimulates the incorporation of cysteine but not of alanine. The present investigation shows that the result indicated by the use of the artificial messenger poly UG applies as well to the synthesis of hemoglobin, thus confirming the validity of the adaptor hypothesis in the synthesis of natural protein.
|Additional Information:||Copyright © 1963 by the National Academy of Sciences Communicated February 25, 1963 The early stages of this work were carried out with the collaboration of Dr. William J. Ray, Jr., whose brilliant suggestion for preparing the sRNAcYSH hybrid by the use of Raney nickel made these experiments possible. We also wish to thank Dr. Frangois Chapeville for a gift of C14CySH-sRNA that was very helpful in the preliminary work. The excellent technical assistance of Mrs. Dorothy Dais is gratefully acknowledged. This research was supported by grants from the National Institutes of Health, U.S. Public Health Service, and the National Science Foundation. One of us (B.W.) is a National Institutes of Health Postdoctoral Research Fellow.|
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|Deposited On:||29 Nov 2006|
|Last Modified:||26 Dec 2012 09:19|
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