Vs. Lalioti et al., PURIFICATION AND CHARACTERIZATION OF A NOVEL POLY(U), POLY(C) RIBONUCLEASE FROM SACCHAROMYCES-CEREVISIAE, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1342(1), 1997, pp. 62-72
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 pu
rified enzyme was able to degrade 26S, 18S and 5S rRNAs as well as mRN
A obtained from in vitro transcription. No catalytic activity was obse
rved when the RNase was incubated with tRNA and double stranded substr
ate. Our findings suggest that this novel RNase may play an important
role in the processing of RNA in Saccharomyces cerevisiae. (C) 1997 El
sevier Science B.V.