Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1971 Mar;68(3):570–573. doi: 10.1073/pnas.68.3.570

Control of Translation by the Conformation of Messenger RNA

Hiroichi Fukami 1, Kazutomo Imahori 1,*
PMCID: PMC388991  PMID: 5276764

Abstract

This study concerns the question of whether protein biosynthesis is controlled by the conformation of messenger RNA. When R17 bacteriophage RNA was first incubated in the presence of Mg++ before being used as messenger in a cell-free system from Escherichia coli, significant changes in the incorporation of phenylalanine and histidine into protein were seen. The amounts of proteins synthesized were also altered. The changes were not due to degradation of R17 RNA nor to denaturation of a contaminating repressor; they could be reversed by appropriate treatment of the RNA. There forms of R17 RNA are therefore postulated for the control mechanism and characterized by their translational behavior. The significance of these forms with respect to their conformation is discussed.

Full text

PDF
570

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Capecchi M. R. Cell-free protein synthesis programmed with R17 RNA: identification of two phage proteins. J Mol Biol. 1966 Oct 28;21(1):173–193. doi: 10.1016/0022-2836(66)90086-6. [DOI] [PubMed] [Google Scholar]
  2. Eggen K., Nathans D. Regulation of protein synthesis directed by coliphage MS2 RNA. II. In vitro repression by phage coat protein. J Mol Biol. 1969 Jan;39(2):293–305. doi: 10.1016/0022-2836(69)90318-0. [DOI] [PubMed] [Google Scholar]
  3. Eggen K., Oeschger M. P., Nathans D. Cell-free protein synthesis directed by colphage MS2 RNA: sequential synthesis of specific phage proteins. Biochem Biophys Res Commun. 1967 Aug 23;28(4):587–597. doi: 10.1016/0006-291x(67)90354-3. [DOI] [PubMed] [Google Scholar]
  4. Engelhardt D. L., Webster R. E., Zinder N. D. Amber mutants and polarity in vitro. J Mol Biol. 1967 Oct 14;29(1):45–58. doi: 10.1016/0022-2836(67)90180-5. [DOI] [PubMed] [Google Scholar]
  5. GESTELAND R. F., BOEDTKER H. SOME PHYSICAL PROPERTIES OF BACTERIOPHAGE R17 AND ITS RIBONUCLEIC ACID. J Mol Biol. 1964 Apr;8:496–507. doi: 10.1016/s0022-2836(64)80007-3. [DOI] [PubMed] [Google Scholar]
  6. Ishida T., Sueoka N. Rearrangement of the secondary structure of the secondary structure of tryptophan sRNA in Escherichia coli. Proc Natl Acad Sci U S A. 1967 Sep;58(3):1080–1087. doi: 10.1073/pnas.58.3.1080. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Lodish H. F. Bacteriophage f2 RNA: control of translation and gene order. Nature. 1968 Oct 26;220(5165):345–350. doi: 10.1038/220345a0. [DOI] [PubMed] [Google Scholar]
  8. Lodish H. F. Independent translation of the genes of bacteriophage f2 RNA. J Mol Biol. 1968 Mar 28;32(3):681–685. doi: 10.1016/0022-2836(68)90351-3. [DOI] [PubMed] [Google Scholar]
  9. Lodish H. F. Specificity in bacterial protein synthesis: role of initiation factors and ribosomal subunits. Nature. 1970 May 23;226(5247):705–707. doi: 10.1038/226705a0. [DOI] [PubMed] [Google Scholar]
  10. Nathans D., Oeschger M. P., Eggen K., Shimura Y. Bacteriophage-specific proteins in e. Coli infected with an RNA bacteriophage. Proc Natl Acad Sci U S A. 1966 Dec;56(6):1844–1851. doi: 10.1073/pnas.56.6.1844. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. OHTAKA Y., SPIEGELMAN S. TRANSLATIONAL CONTROL OF PROTEIN SYNTHESIS IN A CELL-FREE SYSTEM DIRECTED BY A POLYCISTRONIC VIRAL RNA. Science. 1963 Oct 25;142(3591):493–497. doi: 10.1126/science.142.3591.493. [DOI] [PubMed] [Google Scholar]
  12. Steitz J. A., Dube S. K., Rudland P. S. Control of translation of T4 phage: altered ribosome binding at R17 initiation sites. Nature. 1970 May 30;226(5248):824–827. doi: 10.1038/226824a0. [DOI] [PubMed] [Google Scholar]
  13. Zinder N. D., Engelhardt D. L., Webster R. E. Punctuation in the genetic code. Cold Spring Harb Symp Quant Biol. 1966;31:251–256. doi: 10.1101/sqb.1966.031.01.033. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES