Purification and characterization of the precursor tRNA 3'-end processing nuclease from Aspergillus nidulans

Biochem Biophys Res Commun. 1997 Apr 17;233(2):354-8. doi: 10.1006/bbrc.1997.6448.

Abstract

The precursor-tRNA 3'-end processing nuclease activity was purified homogeneously about 15,300 fold from the heat-treated fraction. The precursor-tRNA 3'-end processing nuclease was a single polypeptide of 160,000 Da. This nuclease generates a mature 3'-end of nuclear tRNA(Asp) of Aspergillus nidulans by the endonuclease activity and prefers the 5'-end processed tRNA(Asp) rather than primary precursor-tRNA(Asp) as a substrate. However, this enzyme did not process both primary mitochondrial precursor-tRNA(His) and 5'-end processed mitochondrial precursor-tRNA(His) of A. nidulans.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspergillus nidulans / enzymology*
  • Aspergillus nidulans / genetics
  • Base Sequence
  • Endoribonucleases / genetics
  • Endoribonucleases / isolation & purification*
  • Endoribonucleases / metabolism
  • Molecular Sequence Data
  • Molecular Weight
  • Nucleic Acid Conformation
  • RNA Precursors / metabolism*
  • RNA Processing, Post-Transcriptional*
  • RNA, Transfer, Asp / metabolism*
  • Substrate Specificity
  • Transcription, Genetic

Substances

  • RNA Precursors
  • RNA, Transfer, Asp
  • Endoribonucleases
  • splicing endonuclease