TY - JOUR
TI - Purification and characterization of a novel poly(U), poly(C)
ribonuclease from Saccharomyces cerevisiae
AU - Lalioti, VS
AU - Ballesta, JPG
AU - Fragoulis, EG
JO - Biochimica et Biophysica Acta.  Protein Structure and Molecular Enzymology
PY - 1997
VL - 1342
TODO - 1
SP - 62-72
PB - ELSEVIER SCIENCE BV
SN - 0167-4838
TODO - 10.1016/S0167-4838(97)00078-2
TODO - RNase; endonuclease; mRNA; rRNA; translational control
TODO - A new ribonuclease from Saccharomyces cerevisiae, specific for poly(U)
and poly(C) substrate, was purified near to homogeneity by successive
fractionation with DEAE-Sepharose, Heparin-Sepharose and CM-Sepharose
chromatography. The purified molecule detected by SDS/polyacrylimide gel
electrophoresis has a molecular mass of 29 kDa. The optimum PH for the
enzyme activity is 5.5-7 and its isoelectric point is 7.5. The purified
enzyme was able to degrade 26S, 18S and 5S rRNAs as well as mRNA
obtained from in vitro transcription. No catalytic activity was observed
when the RNase was incubated with tRNA and double stranded substrate.
Our findings suggest that this novel RNase may play an important role in
the processing of RNA in Saccharomyces cerevisiae. (C) 1997 Elsevier
Science B.V.
ER -