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On the Species Specificity of Acceptor RNA and Attachment Enzymes

Benzer, Seymour and Weisblum, Bernard (1961) On the Species Specificity of Acceptor RNA and Attachment Enzymes. Proceedings of the National Academy of Sciences of the United States of America, 47 (8). pp. 1149-1154. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:BENpnas61c

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Abstract

One of the steps in protein biosynthesis appears to be the attachment of each amino acid to a specific acceptor (SRNA) molecule. According to the adaptor hypothesis, each SRNA molecule would then fit to a specific complementary base sequence on a linear RNA template, specifying the sequence of amino acids in the resultant protein [1,2]. An adaptor molecule thus could have two specificities: one recognizing the correct amino acid and activating enzyme; the other, the proper position on the template. The correctness of the amino-acid sequence therefore would depend upon the precision and constancy of the adaptors. However, the structures of the enzymes and adaptors are presumably under the genetic control of the organism and might be subject to heritable modifications. It is therefore conceivable that one or both ends of an adaptor might change sufficiently to cause occasional errors and, in the long run, an alteration of the genetic code might evolve. This notion, prompted by genetic observations [3] which suggested that mutation of a bacterium might modify its translation of genetic information, lead to the present comparison of the specificities of the acceptor RNA and activating enzymes of different organisms. Several differences in specificity have been reported previously. Berg et al. [4] demonstrated that SRNA from Escherichia coli contains two distinguishable acceptors for methionine. An enzyme prepared from yeast could attach methionine to one of these, while the enzyme from E. coli could attach to both. Webster found, in pig liver, a difference between the nuclear and cytoplasmic attachment enzymes for alanine. Rendi and Ochoa [6] noted that, for leucine, the enzymes in yeast and in E. coli could attach only to their homologous SRNA. Furthermore, in the case of leucine, rat liver enzyme and SRNA were interchangeable with those from E. coli. The observations presented below show that whether the enzymes and/or acceptors from two organisms are interchangeable depends upon not only the organisms in question but also the particular amino acid


Item Type:Article
Additional Information:Copyright © 1961 by the National Academy of Sciences Communicated June 26, 1961 We are particularly grateful to Paul Berg for making several manuscripts available to us before publication. The research was supported by grants from the National Science Foundation and the National Institutes of Health.
Record Number:CaltechAUTHORS:BENpnas61c
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:BENpnas61c
Alternative URL:http://www.pnas.org/content/vol47/issue8/
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:6183
Collection:CaltechAUTHORS
Deposited By: Archive Administrator
Deposited On:28 Nov 2006
Last Modified:14 Nov 2014 19:19

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