• We are sorry, but NCBI web applications do not support your browser and may not function properly. More information
Logo of pnasPNASInfo for AuthorsSubscriptionsAboutThis Article
Proc Natl Acad Sci U S A. Aug 1975; 72(8): 3049–3053.
PMCID: PMC432916

Site of aminoacylation of tRNAs from Escherichia coli with respect to the 2'- or 3'-hydroxyl group of the terminal adenosine.


A method is presented by which the site of primary attachment of the amino acids with respect to the 2'- or 3'-hydroxyl group of the terminal adenosine of E. coli tRNAs can be determined. It is found that the aminoacyl-tRNA synthetases (EC 6.1.1.-) with specificity for Arg, Asn, Ile, Leu, Met, Phe, Thr, Trp, and Val attach the amino acid to the 2'-position; those with specificity for Gly, His, Lys, and Ser attach the amino acid to the 3'-position; and that Tyr and Cys can be enzymatically attached to both the 2'- and 3'-positions. Together with previous experiments on yeast aminoacyl-tRNA synthetases, it is now shown that the specificity for one particular hydroxyl group is preserved during the evolution from prokaryotic to eukaryotic systems.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (902K), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Sprinzl M, Scheit KH, Sternbach H, von der Haar F, Cramer F. In vitro in corporation of 2'-deoxyadenosine and 3'-deoxyadenosine into yeast tRNA Phe using t-RNA nucleotidyl transferase, and properties of tRNA Phe -C-C-2'dA and tRNA Phe -C-C-3'dA. Biochem Biophys Res Commun. 1973 Apr 16;51(4):881–887. [PubMed]
  • Sprinzl M, Cramer F. Accepting site for aminoacylation of tRNAphe from yeast. Nat New Biol. 1973 Sep 5;245(140):3–5. [PubMed]
  • Chinali G, Sprinzl M, Parmeggiani A, Cramer F. Participation in protein biosynthesis of transfer ribonucleic acids bearing altered 3'-terminal ribosyl residues. Biochemistry. 1974 Jul 16;13(15):3001–3010. [PubMed]
  • Roe B, Marcu K, Dudock B. The isolation and sequence analysis of transfer RNA: the use of plaskon chromatography (RPC-5). Biochim Biophys Acta. 1973 Aug 10;319(1):25–36. [PubMed]
  • Sternbach H, von der Haar F, Schlimme E, Gaertner E, Cramer F. Isolation and properties of tRNA nucleotidyl transferase from yeast. Eur J Biochem. 1971 Sep 24;22(2):166–172. [PubMed]
  • Yoshikawa M, Kato T, Takenishi T. A novel method for phosphorylation of nucleosides to 5'-nucleotides. Tetrahedron Lett. 1967 Dec;50:5065–5068. [PubMed]
  • Tal J, Deutscher MP, Littauer UZ. Biological activity of Escherichia coli tRNA Phe modified in its C-C-A terminus. Eur J Biochem. 1972 Aug 4;28(4):478–491. [PubMed]
  • Sprinzl M, von der Haar F, Schlimme E, Sternbach H, Cramer F. Incorporation of 5-iodocytidine into yeast tRNAphe with tRNA nucleotidyl transferase in vitro. Eur J Biochem. 1972 Feb 15;25(2):262–266. [PubMed]
  • Ofengand J, Chládek S, Robilard G, Bierbaum J. Enzymatic acylation of oxidized-reduced transfer ribonucleic acid by Escherichia coli, yeast, and rat liver synthetases occurs almost exclusively at the 2'-hydroxyl. Biochemistry. 1974 Dec 17;13(26):5425–5432. [PubMed]
  • ZAMECNIK PC. Unsettled questions in the field of protein synthesis. Biochem J. 1962 Nov;85:257–264. [PMC free article] [PubMed]
  • Chousterman S, Chapeville F. Tyrosyl-tRNA synthetase of Escherichia coli B. Binding of various ligands. Eur J Biochem. 1973 May;35(1):51–56. [PubMed]
  • Beikirch H, von der Haar F, Cramer F. Tyrosyl-tRNA synthetase from baker's yeast. Isolation and some properties. Eur J Biochem. 1972 Mar 27;26(2):182–190. [PubMed]
  • Crothers DM, Seno T, Söll G. Is there a discriminator site in transfer RNA? Proc Natl Acad Sci U S A. 1972 Oct;69(10):3063–3067. [PMC free article] [PubMed]
  • Maelicke A, Sprinzl M, von der Haar F, Khwaja TA, Cramer F. Structural studies on phenylalanine transfer ribonucleic acid from yeast with the spectroscopic label formycin. Eur J Biochem. 1974 Apr 16;43(3):617–625. [PubMed]
  • Sprinzl M. On the structure of phenylalanine tRNA from yeast. Spin-label studies. Eur J Biochem. 1974 Dec 2;49(3):595–605. [PubMed]
  • Cramer F, Erdmann VA, von der Haar F, Schlimme E. Structure and reactivity of tRNA. J Cell Physiol. 1969 Oct;74(2 Suppl):163+–163+. [PubMed]
  • Von Der Haar F, Gaertner E. Phenylalanyl-tRNA synthetase from baker's yeast: role of 3'-terminal adenosine of tRNA-Phe in enzyme-substrate interaction studied with 3'-modified tRNA-Phe species. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1378–1382. [PMC free article] [PubMed]
  • Kisselev LL, Favorova OO. Aminoacyl-tRNA synthetases: sone recent results and achievements. Adv Enzymol Relat Areas Mol Biol. 1974;40(0):141–238. [PubMed]

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


Related citations in PubMed

See reviews...See all...

Cited by other articles in PMC

See all...


Recent Activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...