Abstract
The Pac1 RNase of the fission yeast Schizosaccharomyces pombe is a doublestrand-specific endoribonuclease (dsRNase) whose structure, biochemical properties, and biological functions place it in the RNase III family. This chapter describes the methods that have been used to define the biological functions and biochemical properties of the Pac1 RNase. The pac1 + gene issolated as a multicopy suppressor of snm1, a temperature-sensitive (ts) mutant that maintains reduced steady state amounts of the spliceosomal small nuclear RNAs (snRNAs) and accumulates Y-extended snRNA transcripts. Subsequent work showed that the snml mutation lies in the pac1 + gene and established the requirement for the Pac1 RNase in the 3′ processing of the pre-U2 RNA and presumably other snRNA precursors. Mutant Pac1 alleles, such as snm1, also accumulate Y-extended pre-rRNA, and purified Pac1 RNase cleaves a pre-rRNA at in vivo RNA processing sites. These results established a role for Pac1 in rRNA synthesis, a function shared by all members of the RNase III family.
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