Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 5 April 1963:
Vol. 140. no. 3562, pp. 17 - 26
DOI: 10.1126/science.140.3562.17
Prev | Table of Contents | Next

Articles

Involvement of RNA in the Synthesis of Proteins

The ordered interaction of three classes of RNA controls the assembly of amino acids into proteins

J. D. Watson 1

1 Harvard Biological Laboratories, Cambridge, Massachusetts

We can now have considerable confidence that the broad features of protein synthesis are understood. The involvement of RNA is very much more complicated than was imagined in 1953. There is not one functional RNA. Instead, protein synthesis demands the ordered interaction of three classes of RNA—ribosomal, soluble, and messenger. Many important questions, however, remain unanswered. For instance, there is no theoretical framework for the ribosomal subunits, nor for that matter, do we understand the functional significance of ribosomal RNA. Most satisfying is the realization that all the steps in protein replication will be shown to involve well-understood chemical forces. As yet we do not know all the details. For example, are the DNA base pairs involved in messenger RNA selection of the corresponding amino-acyl-sRNA? With luck, this will soon be known. We can thus have every expectation that future progress in understanding selective protein synthesis (and its consequences for embryology) will have a similarly well-defined and, when understood, easy-to-comprehend chemical basis (62).


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
An Historical Account of Protein Synthesis, with Current Overtones--A Personalized View.
P. C. Zamecnik (1969)
Cold Spring Harb Symp Quant Biol 34, 1-16
   Abstract »    PDF »
On the Mechanism of Coded Binding of Aminoacyl-tRNA to Ribosomes: Number and Properties of Sites.
D. Swan, G. Sander, E. Bermek, W. Kramer, T. Kreuzer, C. Arglebe, R. ZOllner, K. Eckert, and H. Matthaei (1969)
Cold Spring Harb Symp Quant Biol 34, 179-196
   Abstract »    PDF »
Reformation of Functional Liver Polyribosomes from Ribosome Monomers in the Absence of RNA Synthesis.
G. A. Stewart and E. Farber (1967)
Science 157, 67-69
   Abstract »    PDF »
Relationship of Hydroxyproline Excretion in Urine to Collagen Metabolism: Biochemistry and Clinical Applications.
D. J. PROCKOP and K. I. KIVIRIKKO (1967)
Ann Intern Med 66, 1243-1266
   Abstract »    PDF »
Protein Synthesis Enhanced in the Liver of Rats Force-Fed a Threonine-Devoid Diet.
H. Sidransky, T. Staehelin, and E. Verney (1964)
Science 146, 766-768
   Abstract »    PDF »
The Operon: On Its Third Anniversary.
G. S. Stent (1964)
Science 144, 816-820
   PDF »
Molecular Theories of Memory.
W. Dingman and M. B. Sporn (1964)
Science 144, 26-29
   PDF »
Cytodifferentiation and Its Controls.
C. Grobstein (1964)
Science 143, 643-650
   PDF »
Growth and Development of Cultured Plant Cells.
F. C. Steward, M. O. Mapes, A. E. Kent, and R. D. Holsten (1964)
Science 143, 20-27
   PDF »
Protein Biosynthesis: Some Alternative Considerations on the Current Hypothesis.
R. W. Hendler (1963)
Science 142, 402-405
   PDF »
Ribosomal RNA on the Surface of Ribosomes.
M. Santera (1963)
Science 141, 1049-1050
   Abstract »    PDF »
Thoughts on Cancer Research, 1963.
A. GELLHORN (1963)
Ann Intern Med 59, 251-257
   Abstract »    PDF »
The Structure and Function of Polyribosomes.
A. Rich, J. R. Warner, and H. M. Goodman (1963)
Cold Spring Harb Symp Quant Biol 28, 269-285
   Abstract »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)