Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

If You Use a Screen Reader

This content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.

Covalent Joining of Phenylalanine Transfer Ribonucleic Acid Half-Molecules by T4 RNA Ligase

Gabriel Kaufmann and Uriel Z. Littauer
Proceedings of the National Academy of Sciences of the United States of America
Vol. 71, No. 9 (Sep., 1974), pp. 3741-3745
Stable URL: http://www.jstor.org/stable/63869
Page Count: 5
  • Read Online (Free)
  • Subscribe ($19.50)
  • Cite this Item
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Covalent Joining of Phenylalanine Transfer Ribonucleic Acid Half-Molecules by T4 RNA Ligase
Preview not available

Abstract

RNA ligase from T4-phage-infected Escherichia coli cells catalyzes the covalent joining of two polynucleotides that are partially hydrogen-bonded to each other. Two polynucleotide fragments derived from yeast tRNAPhe and consisting of residues 1-36 and 38-74 are covalently joined by the enzyme. The product of the reaction lacks residue Y37 and has an anticodon loop with six nucleotide residues, whereas all tRNA species whose sequences have so far been determined have seven nucleotides in this loop. Evidence is also presented for the formation of a polynucleotide-adenylylate intermediate in the joining reaction, in which a pyrophosphate bond links the 5′-phosphoryl terminus of the polynucleotide and the phosphoryl group of AMP.

Page Thumbnails

  • Thumbnail: Page 
3741
    3741
  • Thumbnail: Page 
3742
    3742
  • Thumbnail: Page 
3743
    3743
  • Thumbnail: Page 
3744
    3744
  • Thumbnail: Page 
3745
    3745