Skip to main content
NCBI home page
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
. 1970 Nov;67(3):1200–1206. doi: 10.1073/pnas.67.3.1200

Seryl-tRNA in Mammalian Tissues: Chromatographic Differences in Brain and Liver and a Specific Response to the Codon, UGA

Dolph Hatfield 1,2, Franklin H Portugal 1,2,*
PMCID: PMC283337  PMID: 5274449

Abstract

Differences in the elution profiles of seryl-tRNAs of beef and of rabbit liver and brain were observed. A species of beef seryl-tRNA obtained by reversed phase column chromatography that responds specifically to the codon UGA was found. In addition, a species of rabbit and of chicken seryl-tRNA that recognizes UGA was found.

Full text

PDF
1200

Images in this article

1205Image
on p.1205

Selected References

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

  1. Adams A., Zachau H. G. Serine specific transfer ribonucleic acids. 15. Some properties of the aggregates from serine specific transfer ribonucleic acids. Eur J Biochem. 1968 Sep 24;5(4):556–558. doi: 10.1111/j.1432-1033.1968.tb00405.x. [DOI] [PubMed] [Google Scholar]
  2. Baliga B. S., Borek E., Weinstein I. B., Srinivasan P. R. Differences in the transfer RNA's of normal liver and Novikoff hepatoma. Proc Natl Acad Sci U S A. 1969 Mar;62(3):899–905. doi: 10.1073/pnas.62.3.899. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Barnett W. E., Brown D. H. Mitochondrial transfer ribonucleic acids. Proc Natl Acad Sci U S A. 1967 Feb;57(2):452–458. doi: 10.1073/pnas.57.2.452. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Brown J. C., Smith A. E. Initiator codons in eukaryotes. Nature. 1970 May 16;226(5246):610–612. doi: 10.1038/226610a0. [DOI] [PubMed] [Google Scholar]
  5. Buck C. A., Nass M. M. Studies on mitochondrial tRNA from animal cells. I. A comparison of mitochondrial and cytoplasmic trna and aminoacyl-tRNA synthetases. J Mol Biol. 1969 Apr 14;41(1):67–82. doi: 10.1016/0022-2836(69)90126-0. [DOI] [PubMed] [Google Scholar]
  6. Capecchi M. R., Klein H. A. Characterization of three proteins involved in polypeptide chain termination. Cold Spring Harb Symp Quant Biol. 1969;34:469–477. doi: 10.1101/sqb.1969.034.01.053. [DOI] [PubMed] [Google Scholar]
  7. Caskey C. T., Beaudet A., Nirenberg M. RNA codons and protein synthesis. 15. Dissimilar responses of mammalian and bacterial transfer RNA fractions to messenger RNA codons. J Mol Biol. 1968 Oct 14;37(1):99–118. doi: 10.1016/0022-2836(68)90076-4. [DOI] [PubMed] [Google Scholar]
  8. Caskey T., Scolnick E., Tompkins R., Goldstein J., Milman G. Peptide chain termination, codon, protein factor, and ribosomal requirements. Cold Spring Harb Symp Quant Biol. 1969;34:479–488. doi: 10.1101/sqb.1969.034.01.054. [DOI] [PubMed] [Google Scholar]
  9. Forney F. W., Markovetz A. J. An enzyme system for aliphatic methyl ketone oxidation. Biochem Biophys Res Commun. 1969 Sep 24;37(1):31–38. doi: 10.1016/0006-291x(69)90876-6. [DOI] [PubMed] [Google Scholar]
  10. Gonano F., Chiarugi V. P. Changes of phenylalanyl-tRNA of Morris hepatoma 5123 revealed by reverse phase chromatography. Exp Mol Pathol. 1969 Feb;10(1):99–103. doi: 10.1016/0014-4800(69)90051-3. [DOI] [PubMed] [Google Scholar]
  11. Holland J. J., Taylor M. W., Buck C. A. Chromatographic differences between tyrosyl transfer RNA from different mammalian cells. Proc Natl Acad Sci U S A. 1967 Dec;58(6):2437–2444. doi: 10.1073/pnas.58.6.2437. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kelmers A. D., Novelli G. D., Stulberg M. P. Separation of transfer ribonucleic acids by reverse phase chromatography. J Biol Chem. 1965 Oct;240(10):3979–3983. [PubMed] [Google Scholar]
  13. Khorana H. G., Büchi H., Ghosh H., Gupta N., Jacob T. M., Kössel H., Morgan R., Narang S. A., Ohtsuka E., Wells R. D. Polynucleotide synthesis and the genetic code. Cold Spring Harb Symp Quant Biol. 1966;31:39–49. doi: 10.1101/sqb.1966.031.01.010. [DOI] [PubMed] [Google Scholar]
  14. Kim W. S. N-formylseryl-transfer RNA. Science. 1969 Feb 28;163(3870):947–949. doi: 10.1126/science.163.3870.947. [DOI] [PubMed] [Google Scholar]
  15. Lebowitz P., Ipata P. L., Makman M. H., Richards H. H., Cantoni G. L. Resolution of cytidine- and adenosine- terminal transfer ribonucleic acids. Biochemistry. 1966 Nov;5(11):3617–3625. doi: 10.1021/bi00875a034. [DOI] [PubMed] [Google Scholar]
  16. Liew C. C., Haslett G. W., Allfrey V. G. N-acetyl-seryl-tRNA and polypeptide chain initiation during histone biosynthesis. Nature. 1970 May 2;226(5244):414–417. doi: 10.1038/226414a0. [DOI] [PubMed] [Google Scholar]
  17. Lindahl T., Adams A., Fresco J. R. Renaturation of transfer ribonucleic acids through site binding of magnesium. Proc Natl Acad Sci U S A. 1966 Apr;55(4):941–948. doi: 10.1073/pnas.55.4.941. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Loehr J. S., Keller E. B. Dimers of alanine transfer RNA with acceptor activity. Proc Natl Acad Sci U S A. 1968 Nov;61(3):1115–1122. doi: 10.1073/pnas.61.3.1115. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Marshall R. E., Caskey C. T., Nirenberg M. Fine structure of RNA codewords recognized by bacterial, amphibian, and mammalian transfer RNA. Science. 1967 Feb 17;155(3764):820–826. doi: 10.1126/science.155.3764.820. [DOI] [PubMed] [Google Scholar]
  20. Mushinski J. F., Potter M. Variations in leucine transfer ribonucleic acid in mouse plasma cell tumors producing kappa-type immunoglobin light chains. Biochemistry. 1969 Apr;8(4):1684–1692. doi: 10.1021/bi00832a051. [DOI] [PubMed] [Google Scholar]
  21. Mäenpä P. H., Bernfield M. R. Quantitative variation in serine transfer ribonucleic acid during estrogen-induced phosphoprotein synthesis in rooster liver. Biochemistry. 1969 Dec;8(12):4926–4935. doi: 10.1021/bi00840a041. [DOI] [PubMed] [Google Scholar]
  22. NIRENBERG M., LEDER P. RNA CODEWORDS AND PROTEIN SYNTHESIS. THE EFFECT OF TRINUCLEOTIDES UPON THE BINDING OF SRNA TO RIBOSOMES. Science. 1964 Sep 25;145(3639):1399–1407. doi: 10.1126/science.145.3639.1399. [DOI] [PubMed] [Google Scholar]
  23. Nirenberg M., Caskey T., Marshall R., Brimacombe R., Kellogg D., Doctor B., Hatfield D., Levin J., Rottman F., Pestka S. The RNA code and protein synthesis. Cold Spring Harb Symp Quant Biol. 1966;31:11–24. doi: 10.1101/sqb.1966.031.01.008. [DOI] [PubMed] [Google Scholar]
  24. Nishimura S., Weinstein I. B. Fractionation of rat liver transfer ribonucleic acid. Isolation of tyrosine, valine, serine, and phenylalanine transfer ribonucleic acids and their coding properties. Biochemistry. 1969 Mar;8(3):832–842. doi: 10.1021/bi00831a011. [DOI] [PubMed] [Google Scholar]
  25. Sambrook J. F., Fan D. P., Brenner S. A strong suppressor specific for UGA. Nature. 1967 Apr 29;214(5087):452–453. doi: 10.1038/214452a0. [DOI] [PubMed] [Google Scholar]
  26. Smith A. E., Marcker K. A. Cytoplasmic methionine transfer RNAs from eukaryotes. Nature. 1970 May 16;226(5246):607–610. doi: 10.1038/226607a0. [DOI] [PubMed] [Google Scholar]
  27. Sueoka N., Hardy J. Deproteinization of cell extract with silicic acid. Arch Biochem Biophys. 1968 May;125(2):558–566. doi: 10.1016/0003-9861(68)90614-0. [DOI] [PubMed] [Google Scholar]
  28. Taylor M. W., Buck C. A., Granger G. A., Holland J. J. Chromatographic alterations in transfer RNA's accompanying speciation, differentiation and tumor formation. J Mol Biol. 1968 May 14;33(3):809–828. doi: 10.1016/0022-2836(68)90321-5. [DOI] [PubMed] [Google Scholar]
  29. Weinstein I. B. A possible role of transfer RNA in the mechanism of carcinogenesis. Cancer Res. 1968 Sep;28(9):1871–1874. [PubMed] [Google Scholar]
  30. Wilcox M., Nirenberg M. Transfer RNA as a cofactor coupling amino acid synthesis with that of protein. Proc Natl Acad Sci U S A. 1968 Sep;61(1):229–236. doi: 10.1073/pnas.61.1.229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Yang S. S., Sanadi D. R. Changes in the distribution of transfer ribonucleic acid species specifically induced by thyroxine. J Biol Chem. 1969 Sep 25;244(18):5081–5083. [PubMed] [Google Scholar]
  32. Yang W. K., Hellman A., Martin D. H., Hellman K. B., Novelli G. D. Isoaccepting transfer RNA's of L-M cells in culture and after tumor induction in C3H mice. Proc Natl Acad Sci U S A. 1969 Dec;64(4):1411–1418. doi: 10.1073/pnas.64.4.1411. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Yang W. K., Novelli G. D. Isoaccepting +RNA's in mouse plasma cell tumors that synthesize different myeloma protein. Biochem Biophys Res Commun. 1968 May 23;31(4):534–539. doi: 10.1016/0006-291x(68)90510-x. [DOI] [PubMed] [Google Scholar]
  34. Yang W. K., Novelli G. D. Multiple isoaccepting transfer RNA's in a muouse plasma cell tumor. Proc Natl Acad Sci U S A. 1968 Jan;59(1):208–215. doi: 10.1073/pnas.59.1.208. [DOI] [PMC free article] [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