Purification and Primary Structure of a New Guanylic Acid Specific Ribonuclease from Pleurotus ostreatus
- 1 July 1994
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 116 (1) , 26-33
- https://doi.org/10.1093/oxfordjournals.jbchem.a124498
Abstract
A guanine nucleotide-specific RNase (RNase Po1) was isolated from caps of the fruit bodies of Pleurotus ostreatus. RNase Po1 is most active towards RNA at pH 8.0. The effect of heating on the molar ellipticity at 210 nm of RNase PO1 showed that RNase Po1 is more stable than RNase T1. The primary structure of RNase Po, was determined to be < ETGVRSCNCAGRSFTGTDVTNAIRSARAGGSGNYPHVYNNFEGFSFSCTPTFFEFPVFRGSVYSFFSPGADRVIYDQSGRFC ACLTHTGAPSTNGFVECRF. It consisted of 101 amino acid residues, with a molecular weight of 10, 760. RNase Poi has relatively higher sequence homology with RNase T1 family RNases. It contains 6 half cystine residues. The locations of four of them are superimposable on those of RNase U1 and RNase U2. The amino acid residues forming the active site of RNase T1 were well conserved in this RNase. Therefore, RNase Poi is a unique member of the RNase T! family in respect of the location of one disulflde bridge, and its stability.Keywords
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