Purification and characterization of the precursor tRNA 3'-end processing nuclease from Aspergillus nidulans.
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.
Han
S J
SJ
Department of Microbiology, College of Natural Sciences, Seoul National University, Korea.
Kang
H S
HS
D001233:Aspergillus nidulans / Q000201:enzymology* / Q000235:genetics; D001483:Base Sequence; D004722:Endoribonucleases / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009690:Nucleic Acid Conformation; D012322:RNA Precursors / Q000378:metabolism*; D012323:RNA Processing, Post-Transcriptional; D012349:RNA, Transfer, Asp / Q000378:metabolism*; D013379:Substrate Specificity; D014158:Transcription, Genetic
D012322:RNA Precursors; D012349:RNA, Transfer, Asp; D004722:Endoribonucleases; C051012:splicing endonuclease