A terminal affair: 3'-end recognition by the human La protein

Trends Biochem Sci. 2006 Jun;31(6):303-5. doi: 10.1016/j.tibs.2006.04.008. Epub 2006 May 6.

Abstract

The La protein, an autoantigen in rheumatic disease, orchestrates several aspects of the metabolism of noncoding RNA molecules. More than 20 years ago it was shown that La primarily binds the 3' UUU-OH tails of nascent transcripts of RNA polymerase III. A recent study now reveals how the structure of the amino-terminal domain of the human La protein achieves specific 3'-end recognition.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Autoantigens / chemistry
  • Autoantigens / genetics
  • Autoantigens / metabolism*
  • Humans
  • Protein Binding
  • Protein Structure, Tertiary
  • RNA Polymerase III / genetics
  • RNA Polymerase III / metabolism*
  • RNA, Untranslated / genetics
  • RNA, Untranslated / metabolism*
  • Rheumatic Diseases / genetics
  • Rheumatic Diseases / metabolism
  • Ribonucleoproteins / chemistry
  • Ribonucleoproteins / genetics
  • Ribonucleoproteins / metabolism*
  • SS-B Antigen

Substances

  • Autoantigens
  • RNA, Untranslated
  • Ribonucleoproteins
  • RNA Polymerase III