Aberrant nuclear trafficking of La protein leads to disordered processing of associated precursor tRNAs

Mol Cell. 2002 May;9(5):1113-23. doi: 10.1016/s1097-2765(02)00533-6.

Abstract

Eukaryotic precursor tRNAs undergo extensive processing prior to nuclear export. The first of multiple factors to interact with pre-tRNAs and other nascent transcripts is the La protein. Using suppressor and wild-type tRNAs, we demonstrate that the normal distribution of cellular end-processed and spliced tRNA species is disordered by La proteins that lack a conserved nuclear retention element. Fission yeast or human La mutants that lack this element enter nuclei and stabilize nascent pre-tRNA but are aberrantly exported and fail to support normal tRNA processing. Instead, anomalous 5' and 3' end-containing, spliced tRNAs accumulate, complexed with the mutant La protein. Thus, appropriate nuclear trafficking by La affects the normal order of pre-tRNA processing.

Publication types

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

MeSH terms

  • Active Transport, Cell Nucleus*
  • Amino Acid Sequence
  • Animals
  • Autoantigens / chemistry
  • Autoantigens / metabolism*
  • Fluorescent Antibody Technique
  • Humans
  • Molecular Sequence Data
  • RNA Precursors / metabolism*
  • RNA Splice Sites
  • RNA Splicing
  • Ribonucleoproteins / chemistry
  • Ribonucleoproteins / metabolism*
  • Schizosaccharomyces / genetics
  • Transfection

Substances

  • Autoantigens
  • RNA Precursors
  • RNA Splice Sites
  • Ribonucleoproteins
  • SS-B antigen