The trimethylguanosine cap structure of U1 snRNA is a component of a bipartite nuclear targeting signal

Cell. 1990 Aug 10;62(3):569-77. doi: 10.1016/0092-8674(90)90021-6.

Abstract

The ability of series of U1 snRNAs and U6 snRNAs to migrate into the nucleus of Xenopus oocytes after injection into the cytoplasm was analyzed. The U snRNAs were made either by injecting U snRNA genes into the nucleus of oocytes or, synthetically, by T7 RNA polymerase, incorporating a variety of cap structures. The results indicate that nuclear targeting of U1 snRNA requires both a trimethylguanosine cap structure and binding of at least one common U snRNP protein. Using synthetic U6 snRNAs, it is further demonstrated that the trimethylguanosine cap structure can act in nuclear targeting in the absence of the common U snRNP proteins. These results imply that U snRNP nuclear targeting signals are of a modular nature.

Publication types

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

MeSH terms

  • Animals
  • Base Sequence
  • Binding Sites
  • Cell Nucleus / metabolism*
  • Female
  • Guanosine / analogs & derivatives*
  • Guanosine / analysis
  • Guanosine / metabolism
  • Molecular Sequence Data
  • Nuclear Proteins / metabolism*
  • Nucleic Acid Conformation
  • Oocytes / metabolism
  • Promoter Regions, Genetic
  • RNA Caps / analysis*
  • RNA, Small Nuclear / biosynthesis
  • RNA, Small Nuclear / genetics*
  • Restriction Mapping
  • Ribonucleoproteins / metabolism*
  • Ribonucleoproteins, Small Nuclear
  • Xenopus

Substances

  • Nuclear Proteins
  • RNA Caps
  • RNA, Small Nuclear
  • Ribonucleoproteins
  • Ribonucleoproteins, Small Nuclear
  • Guanosine
  • N(2),N(2),7-trimethylguanosine